Α-ketoglutarate Transaminase Research Articles

Structural Basis for Phospholyase Activity of a Class III Transaminase Homologue.

Pyridoxal-phosphate (PLP)-dependent enzymes catalyse a remarkable diversity of chemical reactions in nature. A1RDF1 from Arthrobacter aurescens TC1 is a fold type I, PLP-dependent enzyme in the class III transaminase (TA) subgroup. Despite sharing 28 % sequence identity with its closest structural homologues, including β-alanine:pyruvate and γ-aminobutyrate:α-ketoglutarate TAs, A1RDF1 displayed no TA activity. Activity screening revealed that the enzyme possesses phospholyase (E.C. 4.2.3.2) activity towards O-phosphoethanolamine (PEtN), an activity described previously for vertebrate enzymes such as human AGXT2L1, enzymes for which no structure has yet been reported. In order to shed light on the distinctive features of PLP-dependent phospholyases, structures of A1RDF1 in complex with PLP (internal aldimine) and PLP⋅PEtN (external aldimine) were determined, revealing the basis of substrate binding and the structural factors that distinguish the enzyme from class III homologues that display TA activity.

In Pursuit of Genes of Glucose Metabolism

If you don't know where you're going, you might wind up someplace else—Yogi Berra My professional journey, once I accepted the fact that I would not play first base for the Chicago Cubs, was not accomplished in a straight line. I entered medical school intending to become a family physician but soon became interested in research. I took an internal medicine residency at the University of California, San Francisco (UCSF), then a long research fellowship in the nascent field of molecular biology at the National Institutes of Health (NIH), and followed that with training in clinical endocrinology at the University of Wisconsin. I spent the next fifteen years dividing my time between the clinic and laboratory at the University of Iowa. Finally, I decided to concentrate on research and spent the next twenty-three years at Vanderbilt University. For the past eleven years, I have been at the University of Iowa, where I helped establish a new diabetes research center. My research journey also had several different directions. Upon reflection, I guess I ended up “someplace else” by choice, and it certainly has been an interesting trip. It is one I unreservedly recommend.

The dual biosynthetic capability of N-acetylornithine aminotransferase in arginine and lysine biosynthesis.

The genes encoding the seven enzymes needed to synthesize L-lysine from aspartate semialdehyde and pyruvate have been identified in a number of bacterial genera, with the single exception of the dapC gene encoding the PLP-dependent N-succinyl-L, L-diaminopimelate:alpha-ketoglutarate aminotransferase (DapATase). Purification of E. coli DapATase allowed the determination of both the amino-terminal 26 amino acids and a tryptic peptide fragment. Sequence analysis identified both of these sequences as being identical to corresponding sequences from the PLP-dependent E. coli argD-encoded N-acetylornithine aminotransferase (NAcOATase). This enzyme performs a similar reaction to that of DapATase, catalyzing the N-acetylornithine-dependent transamination of alpha-ketoglutarate. PCR cloning of the argD gene from genomic E. coli DNA, expression, and purification yielded homogeneous E. coli NAcOATase. This enzyme exhibits both NAcOATase and DapATase activity, with similar specificity constants for N-acetylornithine and N-succinyl-L,L-DAP, suggesting that it can function in both lysine and arginine biosynthesis. This finding may explain why numerous investigations have failed to identify genetically the bacterial dapC locus, and suggests that this enzyme may be an attractive target for antibacterial inhibitor design due to the essential roles of these two pathways in bacteria.

Light-independent degradation of stromal proteins in intact chloroplasts isolated from Pisum sativum L. leaves: requirement for divalent cations

Intact chloroplasts were isolated from mature pea (Pisum sativum L.) leaves in order to study the degradation of several stromal proteins in organello. Changes in the abundances of ribulose-1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39), phosphoribulokinase (EC 2.7.1.19), glutamine synthetase (EC 6.3.1.2) and ferredoxin-dependent glutamine:α-ketoglutarate aminotransferase (glutamate synthase; EC 1.4.7.1) were detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by Coomassie-staining of the gels or immunoblotting using specific antibodies for the different enzymes. Degradation of several stromal proteins was strongly stimulated when intact chloroplasts were incubated in the light in the presence of dithiothreitol. Since free radicals may artificially accumulate in the chloroplast under such conditions and interfere with the stability of stromal proteins, the general relevance of these processes remains questionable. In the absence of light, proteolysis proceeded slowly in isolated chloroplasts and was not stimulated by dithiothreitol. Inhibition by ethylenediaminetetraacetic acid (EDTA), 1,10-phenanthroline or excess zinc ions as well as the requirement for divalent cations suggested that a zinc-containing metalloprotease participated in this process. Furthermore, light-independent degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase and phosphoribulokinase was enhanced in chloroplasts isolated from leaves in which senescence was accelerated by nitrogen starvation. Our results indicate that light-independent stromal protein degradation in intact chloroplasts may be analogous to proteolysis that occurs in intact leaves during senescence.

Regulation of glutamate and GABA transport by adrenoceptors in primary astroglial cell cultures

Un astrocytes grown in primary cultures from cerebral cortex of neonatal rats, α1-adrenoceptors regulate the active uptake of glutamate followed by an activation of glutamic oxaloacetate transaminase (GOT; EC 2.6.1.1) and a slight activation of glutamine synthetase (GS; EC 6.3.1.2) activity. The β-adrenoceptors regulate the active uptake of GABA, and this is followed by an activation of γ-aminobutyric acid α-ketoglutarate transaminase (GABA-T; EC 2.6.1.19.). The data suggest that astrocyte adrenoceptors may modulate neurotransmitter induced neuronal excitability.

The Effect of Dietary Protein on Nitrogen and Sulfur Metabolism in Portacaval-Shunted Rats

The effect of varying the amount of protein in the diet on postoperative recovery, plasma ammonia, urinary orotic acid and metabolism of sulfur-containing amino acids was examined in rats with portacaval shunts (PCS). Food intake and weight gain were lower in both PCS and control rats fed a low (6%) casein diet unsupplemented with methionine compared with rats fed an adequate (18%) casein diet. PCS rats fed 60% casein ate slightly less and took longer to recover their preoperative body weight compared to 60% controls. Shunted rats were consistently hyperammonemic and orotic aciduric compared to controls. Increasing protein in the diet elevated plasma ammonia and urinary orotic acid in all rats to levels above those of the rats fed 18% casein, but the effect was greater in rats with PCS. After i.p. injection of L-[35S]methionine or L-[35S]cysteine, urinary 35S and [35S]sulfate excretion increased and [35S]taurine and total taurine excretion decreased in all rats fed 60% casein. These changes are consistent with our observation that hepatic activities of cysteine dioxygenase and cysteine sulfinate:α-ketoglutarate aminotransferase increased and that of cysteine sulfinate decarboxylase decreased in rats fed the high protein diet. The effect of dietary treatment on both urinary taurine excretion and decarboxylase activity was greater in PCS rats than in controls. Although PCS rats fed a high protein diet may have a decreased taurine-synthesizing capability compared to controls, their ability to oxidize a methionine or cysteine load to sulfate is not compromised by feeding either an 18 or 60% casein diet.

Regional and subcellular distribution of enzymes of branched-chain amino acid metabolism in brains of normal and diabetic rats.

Branched-chain-amino-acid:alpha-ketoglutarate transaminase and branched-chain alpha-ketoacid dehydrogenase have been assayed in brains of control and of streptozotocin-induced diabetic rats. Enzyme activities were measured in five distinct regions of the brain: cerebellum, pons + medulla, midbrain, thalamus + hypothalamus, and telencephalon. Subcellular distribution of these enzymes in whole brain was assessed by fractionating brain homogenate into cytoplasm, free mitochondria, and synaptosomes. The following enzymes were used as markers: lactate dehydrogenase for cytoplasm, glutamate dehydrogenase for mitochondria, and glutamate decarboxylase for synaptosomes. The activity of the branched-chain amino acid transaminase in all brain regions was considerably higher than that of the branched-chain alpha-ketoacid dehydrogenase. While the highest activity of the transaminase occurred in brain-stem regions, the highest activity of the dehydrogenase was present in cerebellum and telencephalon. Diabetes did not affect the activity of the transaminase, but it caused a decrease in the total activity of the dehydrogenase in midbrain and in thalamus + hypothalamus. The transaminase was localized in the cytoplasmic fraction of whole brain, while the dehydrogenase was enriched in the free mitochondria.

83] Kynurenine aminotransferase from kidney supernatant

This chapter provides an overview of the kynurenine aminotransferase from kidney supernatant. L-kynurenine: α-ketoglutarate aminotransferase (cyclizing) activity of rat kidney supernatant, an enzyme in tryptophan catabolism, copurifies with the activity of α-aminoadipate: α-ketoglutarate aminotransferase. The presence of aminoadipate (kynurenine) aminotransferase in kidney represents an enzyme associated with lysine catabolism rather than with tryptophan degradation. α-aminoadipate (kynurenine) aminotransferase also catalyzes aminotransfer of 3,5-diiodotyrosine (halogenated tyrosine aminotransferase) suggesting a possible role in thyroid hormone metabolism. The reactions catalyzed by the kynurenine and halogenated tyrosine aminotransferase activities are presented diagrammatically. α-aminoadipate (kynurenine):α-ketoglutarate aminotransferase activity is also present in rat kidney mitochondria and the supernatant and mitochondrial fractions of rat liver. The activity of the L-α-aminoadipate aminotransferase is measured by the rate of disappearance or appearance of α-ketoglutarate with glutamate dehydrogenase. The chapter also reviews the kynurenine aminotransferase assay. The activity of kynurenine aminotransferase is measured spectrophotometrically by following the appearance of kynurenate.

Developmental pattern, tissue distribution, and subcellular distribution of cysteine: alpha-ketoglutarate aminotransferase and 3-mercaptopyruvate sulfurtransferase activities in the rat.

The tissue distribution, the subcellular distribution in liver, and the developmental patterns of cysteine:alpha-ketoglutarate aminotransferase (CAT) and 3-mercaptopyruvate sulfurtransferase (MPST) activities were determined in rats of the Sprague-Dawley strain. CAT activity was highest in heart and liver, whereas MPST activity was highest in liver and kidney. CAT activity was located primarily in the mitochondrial fraction with a low level of activity in all other fractions. MPST activity was located in both the mitochondrial and cytosolic fractions. The specific activity of CAT and MPST generally increased in rat liver, heart, and kidney during the developmental period from 18 days of gestation to 26 days after birth. Peak CAT-specific activity occurred at about 4 days of age and peak MPST activity occurred at about 21 days of age; peak activity of both CAT and MPST exceeded the adult specific activities. The distribution and developmental pattern of hydrogen sulfide production from cysteine, catalyzed by the coupled activities of CAT and MPST, was similar to those of CAT activity.

Distribution of .OMEGA.-amino acid: Pyruvate transaminase and aminobutyrate: .ALPHA.-Ketoglutarate transaminase in microorganisms.

The distribution of ω-ammo acid transaminases in microorganisms was investigated. ω-Amino acid : pyruvate t ansaminase (ω-APT) was found bacteria and yeasts, but not in actinomycetes and fungi. On the contrary, aminobutyrate : α-ketoglutarate transaminase (GABA-T) was shown in most of the microorganisms from bacteria to fungi. β-Alanine is a preferred amino donor for the ω-APT reaction. Although bacterial and yeast GABA-T are inactive for β-alanine, fungal and actinomycete enzymes react with this compound and γ-aminobutyrate. In comparing these results with those of plant and mammalian enzymes, two different pathways of ω-amino acid metabolism are suggested for bacteria, yeast and plants, i.e. one for β-alanine and the other for γ-aminobutyrate, catalyzed by ω-APT and GABA-T, respectively. In actinomycetes, fungi, and mammals GABA-T may be involved in the metabolism of both ω-amino acids. In addition, evolutionary changes of ω-amino acid transaminases are discussed.

γ-Aminobutyrate:α-Ketoglutarate aminotransferase from Pseudomonas sp. F-126: Purification, crystallization, and enzymologic properties

γ-Aminobutyrate:α-ketoglutarate aminotransferase was purified from Pseudomonas sp. F-126 and crystallized. The crystalline enzyme is homogenous by the criteria of disc electrophoresis and ultracentrifugation ( s 0 20,w = 8.8 S). Molecular weights of 176,000 and 178,000 were obtained by gel filtration and ultracentrifugal sedimentation equilibrium methods, respectively. The enzyme exhibits absorption maxima at 415, 278, and 258 nm with shoulders at 284, 270, and 265 nm. The enzyme catalyzes the transamination of various ω-amino acid with α-ketoglutarate; γ-aminobutyrate is the best amino donor. The Michaelis constants are 2.8 m m for α-ketoglutarate and 4.1 m m for γ-aminobutyrate. In addition to ω-amino acids both isomers of ornithine and lysine and their decarboxylated product; i.e., putrescine and cadaverine, can serve as amino donors. No activity was observed with β-alanine. The enzyme has a maximum activity in the pH range of 8.5–9.0 and at 60 °C. The enzyme is stable at pH 6.0–10.0 at temperatures up to 65 °C. Pyridoxal 5′-phosphate protects the enzyme from heat inactivation. Carbonyl reagents and sulfhydryl reagents inhibit the enzyme activity but the enzyme inactivated by these reagents was reactivated by incubation with pyridoxal 5′-phosphate and thiol compounds, respectively. Chelating agents, nonsubstrate l- and d-α-amino acids, and metal ions except cupric ion showed no effect on the enzyme activity.

Induction of tyrosine α-ketoglutarate transaminase by primycin in rat liver

Induction of tyrosine α-ketoglutarate transaminase by primycin in rat liver

On the mechanism of pyridoxal phosphate-related convulsions as implicated in enhanced transport of GABA

The intracisternal injection of pyridoxine or pyridoxal phosphate has been shown to result in status epilepticus, which is preventable or reversible by GABA. Since pyridoxal phosphate and pyridoxamine phosphate serve as coenzymes for glutamic acid decarboxylase and γ-aminobutyric acid α-ketoglutarate transaminase respectively, and since alteration in GABA level produces convulsions, the effect of Vitamin B 6 on the uptake of GABA in synaptosomes was investigated. It was found that the B 6 vitamers, pyridoxal, pyridoxamine, pyridoxal phosphate or pyridoxamine phosphate; the vitamin B 6 antimetabolite such as deoxypyridoxine; and the vitamin B 6 depletors namely, cycloserine or isoniazid failed to alter the uptake of GABA into synaptosomes isolated from either the cerebral cortex or the hippocampus. On the other hand, pyridoxal or pyridoxal phosphate in a concentration of 1 mM enhanced GABA uptake in nuclear free crude homogenates of the cerebral cortex. These results do not support the direct involvement of B 6 derivatives in the transport of GABA. The effect of pyridoxal phosphate on the specific binding of GABA may clarify further the mechanism of pyridoxal phosphate-related convulsions

The distribution of taurine, cysteinyl sulphinilic acid decarboxylase and crysteinyl sulphinlic acid α-ketoglutarate transaminase in the rat olfactory bulb and olfactory nucleus

Taurine, a putative neurotransmitter, cysteinyl sulphinlic acid α-ketogluraric acid transaminase (CSA-T) and cysteinyl sulphinlic acid decarboxylase (CSA-D) were measured in the different structures of the rat olfactory bulb and olfactory nucleus. It appears there are significant differences between the level of taurine in internal layers (mitral cells, plexiform) and external layer such as fibrorum. The CSA-T and CSA-D activities followed approximately the distribution of taurine in the different areas of the rat olfactory bulb and nucleus. A very high activity of CSA-T was present in all areas studied and a role for the enzyme is proposed. The cellular distribution of CSA-T, CSA-D and taurine is compared with the distribution in retina.

Properties of taurine : α-ketoglutarate aminotransferase of Achromobacter superficialis Inactivation and reactivation of enzyme

The activity of taurine : α-ketoglutarate aminotransferase (taurine : 2-oxoglutarate aminotransferase, EC 2.6.1.55) from Achromobacter superficialis is significantly diminished by treatment of the enzyme with (NH 4) 2SO 4 in the course of purification, and recovered by incubation with pyridoxal phosphate at high temperatures such as 60°C. The inactive form of enzyme absorbing at 280 and 345 nm contains 3 mol of pyridoxal phosphate per mol. The activated enzyme contains additional 1 mol of pyridoxal phosphate with a maximum at 430 nm. This peak is shifted to about 400 nm as a shoulder by dialysis of the enzyme, but the activity is not influenced. The inactive form is regarded as a partially resolved form, i.e. a semiapoenzyme. the enzyme catalyses transamination of various ω-amino acids with α-ketoglutarate, which is the exclusive amino acceptor. Hypotaurine, dl-β-aminoisobutyrate, β-alanine and taurine are the preferred amino donors. The apparent Michaelis constants are as follows; taurine 12 mM, hypotaurine 16 mM, dl-β-aminoisobutyrate 11 mM, β-alanine 17 mM, α-ketoglutarate 11 mM and pyridoxal phosphate 5 μM.

Oxidation of leucine by heart and muscle homogenates of the cardiomyopathic hamster

The oxidation of leucine was measured in heart and muscle homogenates of cardiomyopathic and normal hamsters at three ages. Leucine oxidation was significantly decreased in heart but increased in muscle. The activity of leucine α-ketoglutarate transaminase was unchanged in heart but increased in muscle. It is concluded that catabolism of amino acids may contribute significantly to the energy requirements of the diseased animals.

Metabolisme du ?-aminobutyrate chez Agaricus bisporus Lge.

Transamination between γ-aminobutyrate and α-ketoglutarate provides a pathway for the utilization of γ-aminobutyrate in fruit-bodies of Agaricus bisporus Lge. This reaction leads to the formation of succinic semialdehyde, a metabolic intermediate in the metabolism of γ-aminobutyrate to succinate in the cell. γ-aminobutyrate: α-ketoglutarate aminotransferase (E.C. 2.6.1.19) was sonically extracted from the mitochondrial fraction and partially purified by DEAE-cellulose column chromatography. Aminotransferase had a pH optimum between 8.1 and 8.5 and did not require pyridoxal-phosphate in vitro; however, the enzyme was inhibited by carbonyl-trapping reagents such as pyridoxal-phosphate activated enzymes. The Km values for γ-aminobutyrate and α-ketoglutarate calculated from Lineweaver-Burk plots were 2.2×10-4 M and 2.5×10-3 M, respectively. The transaminase was specific for α-ketoglutarate but not for γ-aminobutyrate; aspartate, α-alanine and δ-aminovalerianate also functioned as amino-group donors. Activity of the enzyme was not influenced by the addition of carboxylic acids of the Krebs cycle. The reversal of the transamination reaction showed optimal rates at pH 9.0–9.3. Some considerations on the physiological significance of these results are given.

Separation of L-phenylalanine: Pyruvate transaminase and L-phenylalanine: α-ketoglutarate transaminase by Sephadex-electrophoresis

By means of a Sephadex-electrophoresis column, L-phenylalanine: pyruvate transaminase (PPT) was separated from L-phenylalanine: α-ketoglutarate transaminase (PKT) from rat liver. These enzymes differed in heat lability in vitro and in their inducibility by glucagon in vivo . PPT was heat-stable and was induced by chronic glucagon injection. On the other hand, PKT was heat-labile and was not induced by glucagon under the experimental conditions used. These studies provide evidence that distinct enzymes catalyze the transamination of phenylalanine with pyruvate or with α-ketoglutarate as the amino acceptor.

Metabolism of tyrosine and phenylalanine in Trtpanosoma brucei gambiense

1. 1. Soluble extracts of Trypanosoma brucei gambiense were found to contain high activity of the enzyme l-tyrosine: α-ketoglutarate aminotransferase (EC 2.6.1.5) amounting to 1.69 μmoles of tyrosine transaminated/mg. of protein/hour. 2. 2. Living, sonicated and sonicated + dialyzed preparations of this protozoan metabolized [ 14C] tyrosine to p-hydroxyphenylpyruvate and p-hydroxyphenyIlactate and [ 14C] phenylalanine to phenylpyruvate. Hydroxylation of tyrosine to 3,4-dihydroxyphenyIalanine (DOPA) and of phenylalanine to tyrosine, was not detected. 3. 3. Transamination of tyrosine by dialyzed enzyme preparations required both α-ketoglutarate and pyridoxal phosphate, while transamination of phenylalanine required only α-ketoglutarate. Two different transaminases appear to be responsible for the transamination of these two amino acids. 4. 4. Synthesis of p-hydroxyphenyllactate from [ 14C] tyrosine required NADH. 5. 5. Noradrenaline, DOPA and α-methyl p-tyrosine all inhibited the tyrosine aminotransferase to differing extents.

Transamination of hypotaurine by taurine:α-ketoglutarate aminotransferase

FEBS LettersVolume 45, Issue 1-2 p. 111-113 Full-length articleFree Access Transamination of hypotaurine by taurine:α-ketoglutarate aminotransferase H. Tanaka, H. Tanaka Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University, Uji, Kyoto-Fu 611, Japan Department of Pharmaceutical Biology, Kyoto College of Pharmacy, Yamashina, Kyoto 607, Japan. Search for more papers by this authorS. Toyama, S. Toyama Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University, Uji, Kyoto-Fu 611, Japan Department of Agricultural and Biological Chemistry, Ryukyu University, Naha, Okinawa 903, Japan. Search for more papers by this authorH. Tsukahara, H. Tsukahara Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University, Uji, Kyoto-Fu 611, JapanSearch for more papers by this authorK. Soda, Corresponding Author K. Soda Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University, Uji, Kyoto-Fu 611, JapanTo whom correspondence should be sent.Search for more papers by this author H. Tanaka, H. Tanaka Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University, Uji, Kyoto-Fu 611, Japan Department of Pharmaceutical Biology, Kyoto College of Pharmacy, Yamashina, Kyoto 607, Japan. Search for more papers by this authorS. Toyama, S. Toyama Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University, Uji, Kyoto-Fu 611, Japan Department of Agricultural and Biological Chemistry, Ryukyu University, Naha, Okinawa 903, Japan. Search for more papers by this authorH. Tsukahara, H. Tsukahara Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University, Uji, Kyoto-Fu 611, JapanSearch for more papers by this authorK. Soda, Corresponding Author K. Soda Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University, Uji, Kyoto-Fu 611, JapanTo whom correspondence should be sent.Search for more papers by this author First published: September 01, 1974 https://doi.org/10.1016/0014-5793(74)80823-9Citations: 9 AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL No abstract is available for this article. References 1 S. Ouchi, J. Biochem. (Tokyo), 46, (1959), 765– 769. 2 B. Bergeret, F. Chatagner, Biochim. Biophys. Acta, 14, (1954), 543– 550. 3 D. Cavalli, B. Mondovi, C. DeMarco, J. Biol. Chem., 216, (1955), 577– 582. 4 A. Meister, 2nd edn Biochemistry of the Amino Acids 799-811, (1965), Academic Press New York 1– 5 K. Sumizu, Biochim. Biophys. Acta, 63, (1962), 210– 212. 6 S. Toyama, K. Soda, J. Bacteriol., 109, (1972), 533– 538. 7 S. Toyama, H. Misono, K. Soda, Biochem. Biophys. Res. Commun., 46, (1972), 1374– 1379. 8 D. Cavallini, B. Mondovi, C. DeMarco, G.B. Brown Biochemical Preparations 10, (1965), John Wiley & Sons New York 72– 75. 9 K. Soda, T. Tochikura, H. Katagiri, Agr. Biol. Chem., 25, (1961), 811– 819. 10 K. Soda, S. Toyama, H. Misono, T. Hirasawa, K. Asada, Agr. Biol. Chem., 37, (1973), 1393– 1400. 11 P.W. West, G.C. Gaeke, Anal. Chem., 28, (1956), 1816– 1819. 12 P. Fromageot, F. Chapeville, L. Petir, Biochim. Biophys. Acta, 23, (1957), 12– 17. Citing Literature Volume45, Issue1-2September 01, 1974Pages 111-113 ReferencesRelatedInformation