Esterase A2 Research Articles

Genetic and physiological variation among bean lines resistant and susceptible to bean anthracnose

Electrophoresis was used to determine genetic and or biochemical variation, if any, among bean lines resistant and susceptible to anthracnose. This was based on two enzyme systems: peroxisase and esterase. It was revealed that resistant and suceptible plants differed in their band patterns and intensities. Band intensity differences occurred mainly among monomorphic bands with higher intensities expressed by susceptible plants, while band pattern differences were expressed both by resistant and susceptible plants. These differences appeared only at certain stages of development. These stages were identified as 3 and 40 days after emergence and were considered as critical stages for screening purposes. The peroxidase isozyme A5 and the esterase isozyme C1 at 3 days, and the peroxidase band C1 and esterase bands A1 and A2 at 40 days were important because these differences could be used as 'genetic/biochemical' markers for screening the population for resistance. Thus, electrophoretic differences could be used as a screening aid and this could save time and effort in breeding programmes. Comparisons between inoculated and non-inoculated leaves of resistant and susceptible lines indicated that infection induced changes in both the amount and kind of peroxidases even before symptoms of the disease appeared. However, there were no specific differences between resistant and susceptible lines, indicating that resistant and susceptible lines responded to infection in the same manner.

Proteins binding to kallikrein and esterase A2 in the urine of salt-sensitive and salt-resistant rats.

Iodine-labeled ([125I]) rat urinary kallikrein and rat urinary TAME esterase A2 were used as probes to look for urinary and plasma proteins that bind to these enzymes. Such proteins are presumptive enzyme inhibitors. Complexes formed with labeled enzymes were identified by polyacrylamide gel electrophoresis followed by autoradiography. Urine from young (6 weeks old) Dahl salt-sensitive (S) rats showed no, or only traces, of protein binding to kallikrein. Concomitant with the slow development of hypertension and proteinuria in S rats fed normal rat chow, one of the six kallikrein-binding proteins demonstrable in plasma was readily found in S-rat urine. This kallikrein-binding protein was called "KBP-1." R rats showed either no or much less KBP-1 in the urine, compared to S rats up to 5 months of age. A partly purified preparation of KBP-1 was shown to inhibit the TAME esterase activity of rat urinary kallikrein in the radiometric TAME assay. Urine of proteinuric S rats also contained two TAME esterase-binding proteins, TEBP-1 and TEBP-2, detected with the [125I]-esterase A2 probe. As S rats aged from 3 to 8 months, free KBP-1 disappeared from the urine in spite of increased and marked proteinuria and the continued presence of KBP-1 in plasma. Concomitant with this age-related loss of urinary KBP-1 there was a marked shift in S urinary proteins binding to [125I]-esterase A2 from TEBP-1 to TEBP-2. It was speculated that KBP-1 and TEBP-1 were the same protein detectable with either labeled kallikrein or labeled esterase A2. The concomitant disappearance of free KBP-1 (TEBP-1) and the appearance of free TEBP-2 in the urine of old, hypertensive, proteinuric S rats suggests that: 1) most of the KBP-1 (TEBP-1) is bound to enzyme(s) in old rats; or 2) KBP-1 (TEBP-1) is largely converted to TEBP-2 in old rats; or 3) both are true and that binding of KBP-1 (TEBP-1) to enzymes is associated with the generation of TEBP-2.

Evidence for an androgen-dependent urinary arginine esterase in the rat: separation from other urinary arginine esterases including kallikrein.

DEAE-Sephadex chromatography of male rat urine resolved three peaks of arginine esterase activity using the synthetic substrate alpha-N-p-tosyl-L-arginine methyl ester . HCl (Tos-Arg-O-Me). Esterase activity in peak 1 (esterase A1 fraction) was present in sexually mature males, but it was not found in mature females, castrated mature males, or sexually immature males. Urinary esterase A1 activity could be restored in castrated mature males by the administration of testosterone, and it is, therefore, androgen dependent. Esterase A1 activity was undetectable and could not be induced in females by daily doses of testosterone (up to 20 mg/day). The second urinary esterase peak (esterase A2 fraction) and the third peak (urinary kallikrein) were found in both male and female rats. Molecular sieve chromatography of esterase fractions A1, A2, and kallikrein, as determined by Sephacryl S-200 chromatography, gave single peaks of activity. Molecular weights were estimated to be 28,500, 42,000, and 41,500, respectively. Kinin-generating activities of esterases A1, A2, and kallikrein were also determined using dog plasma substrate. Esterase A1 fraction had no kinin-generating activity, while esterase A2 fraction demonstrated significant activity but was 12 times less active than kallikrein per Tos-Arg-O-Me esterase unit. Esterase A2 fraction could not induce direct contraction of the rat uterus, and A2 did not cause a transient decrease in rat blood pressure when injected iv, both of which are criteria for kallikrein activity. It is concluded that the androgen-dependent Tos-Arg-O-Me esterase has properties quite different from both esterase A2 and kallikrein. Esterase A2 appears to be similar to the esterase A described in female rat urine by Nustad and Pierce.

Effects of rat urinary arginine esterases on rat kidney to release renin.

Urinary kallikrein has been reported to activate human plasma inactive renin. Our previous report suggests that rat urinary kallikrein releases active renin from rat renal cortical slices. Recently, McPartland et al. were able to separate the A esterase activity of male rat urine into two components: A1 and A2. To evaluate whether these other urine arginine esterases release renin from the kidney, esterases A1 and A2 were isolated from male rat urine using DEAE-Sephadex chromatography and superfused to rat renal cortical slices. The renin-stimulating action of these enzymes was compared to that of rat urinary kallikrein. Rat urinary kallikrein stimulated renin release in a dose-dependent fashion between 70--140 milliesterase units (mEU)/ml. Esterase A2 dose stimulated renin release significantly between 120--140 mEU/ml. However, esterase A1 did not stimulate renin release at concentrations between 70--140 mEU/ml. Although Trasylol completely abolished kallikrein and esterase A2 stimulated renin release, soybean trypsin inhibitor blocked only esterase A2-stimulated renin release. The physiological role and site of origin of the A1 and A2 esterases is unknown. However, similar to kallikrein, esterase A2 is a potent stimulator of renin release and may be physiologically important for the release and activation of renin in the kidney.

New studies on the esterase D polymorphism in South American Indians.

A total of 2,490 South American Indians affiliated with 10 tribes were studied for esterases A1, A2, A3, B, D, and carbonic anhydrases 1 and 2. Wide variation was observed in the prevalence of ESD1, the extreme values being 0.44, encountered among the Xikrin, and 0.95, found among the Cashinawa. Seven of the 10 frequencies fell within the interval of 0.66--0.87. These results were integrated with those of earlier surveys. In a general way we observe lower values in the eastern and Atlantic Coast groups, but this is mainly due to the low frequencies found among the Gê tribes and the Caingang, who speak a language which has many affinities with Gê. High prevalences were observed among the tropical forest tribes. A fair amount of intervillage, intratribal variation was found among the Ticuna and Caingang. No variability was detected in the A1, A2, A3, B esterases. In the carbonic anhydrases we confirmed the presence of a "private polymorphism" among the Baniwa.

Kininogenase activity and kinin-like substance in the venomous spicules and spines of lepidopteran larvae.

Of the medically important caterpillars of Lepidopteran insects (moths and butterflies) in Japan, some species of the genus Euproctis (tussock moth) and three kinds of slug moths, Parasa consocia, Parasa sinica, Cnidocampa flavescens, are known to be the most harmful. Recently, the pioneer work was performed by de Jong and Bleumink (1–2) concerning the spicule venom of the brown tail moth, E. chrysorrhoea, and they found the presence of enzymic activities of protease, esterase and phospholipase A2 in its extract. However, there is little knowledge about the nature of the venoms involved in the venomous spicules and spines of the above insects.KeywordsLepidopteran InsectCrude VenomLepidopteran LarvaLower Molecular FractionTussock MothThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Decreased activity of peptide-elongation factors after treatment with cholesterol esterase

1. Peptide-elongation factors were purified from rat liver and treated with cholesterol esterase and phospholipase A2 immobilized on Sepharose 4B. 2. Binding of L-[3H]-phenylalanyl-tRNA to 40S ribosomal subunits was decreased by approx. 70% and to polyribosomes by 30% in the presence of the binding factor incubated with cholesterol esterase. Treatment of this factor with immobilized phospholipase A2 decreased the binding to smaller ribosomal subunits by only about 15%. 3. Poly(U)-dependent phenylalanine polymerization by ribosomal subunits was decreased to approx. 30% of its original value by treatment of both elongation factors with cholesterol esterase. 4. The normal activity of esterase-treated elongation factor in both the binding reaction and peptide-elongation assay was fully recovered by the addition of cholesteryl 14-methyl-hexadecanoate. 5. Different classes of lipids present in peptide-elongation factor 1 have apparently different functions. Whereas phospholipids are required to maintain the strcture of heavy aggregates of this factor, the presence of cholesteryl 14-methylhexadecanoate is obviously necessary for the normal function of peptide-elongation factors.

Genetic studies of the Macushi and Wapishana Indians

Blood samples from 509 Macushi and 623 Wapishana Amerindians of of Northern Brazil and Southern Guyana have been analyzed with reference to the occurrence of rare variants and genetic polymorphisms of the following 25 systems: (i) Erythrocyte enzymes: acid phosphatase-1, adenosine deaminase, adenylate kinase-k, carbonic anhydrase-1, carbonic anhydrase-2, esterase A1,2,3, esterase D, galactose-1-phosphate uridyltransferase, isocitrate dehydrogenase, lactate dehydrogenase, malate dehydrogenase, nucleoside phosphorylase, peptidase A, peptidase B, phosphoglucomutase 1, phosphoglucomutase 2, phosphogluconate dehydrogenase, phosphohexoseisomerase, triosephosphate isomerase and (ii) Serum proteins: albumin, ceruloplasmin, haptoglobin, hemoglobin A2 and transferrin. Fifteen different rare variants were detected, involving 11 of these systems. In addition, a previously undescribed variant of ESA 1,2,3 which achieves polymorphic proportions in both these tribes is described. Excluding this variant, the frequency of rare variants is 1.1/1000 in 12510 determinations in the Macushi and 4.7/1000 in 15396 determinations in the Wapishana. The ESA 1,2,3 polymorphism was not observed in 382 Makiritare, 232 Yanomama, 146 Piaroa, 404 Cayapo, 190 Kraho and 112 Moro. Irregularities in the intratribal distribution of this polymorphism in the Macushi and Wapishana render a decision as to the tribe of origin impossible at present. Gene frequencies are also given for previously described polymorphisms of 5 systems: haptoglobin, phosphoglucomutase 1, erythrocyte acid phosphatase, esterase D, and galactose-1-phosphate-uridyl-transferase.