Destruction Of Tyrosine Research Articles

The Radiation-induced Inactivation of External Yeast Invertase in Dilute Aqueous Solution

The inactivation of external yeast invertase by irradiation in dilute aqueous solution has been investigated. The contributions of the individual radical species from water radiolysis to inactivation and amino acid degradation were estimated from the results of experiments in which solutions were saturated with nitrogen, nitrous oxide or oxygen, and on addition of hydroxyl radical scavengers. Under conditions where inactivation by hydroxyl radicals predominates, the rate of inactivation increased with increasing dose, indicating that in the initial stages of the radiolysis the mannose-rich oligosaccharide chains of the glycoprotein protect the polypeptide chain from radical attack. Amino acid analysis of the irradiated external invertase showed that there was significant destruction of tyrosine, phenylalanine, methionine and histidine residues. Destruction of methionine and histidine residues may be responsible for the free radical-induced inactivation of this enzyme.

Presence of sodium azide during acid hydrolysis of protein samples causes the destruction of tyrosine, phenylalanine and histidine

Presence of sodium azide during acid hydrolysis of protein samples causes the destruction of tyrosine, phenylalanine and histidine

Primary structure of the L chain from a rabbit homogeneous antibody to streptococcal carbohydrate. I. Purification of antibody and sequence determination of peptides from alpha-chymo-tryptic and thermolytic digests.

Primary structural studies have been carried out on the light chain of a homogeneous rabbit antibody to Group C streptococcal carbohydrate. Approximately 20 g of this antibody were obtained by multiple exchange transfusions at the peak of the antibody response. The isolated antibody was homogeneous by several antigenic and chemical criteria. The light chain was isolated and modified, and then digested with alpha-chymotrypsin or thermolysin. The resulting peptides were isolated by gel filtration, paper electrophoresis, and paper chromatography. The amino acid sequences of these peptides were determined by Edman degradation plus dansylation. This supplied sufficient information to assign approximately 90 percent of the residues in the chain. The destruction of tyrosine during acid hydrolysis of peptides which had been eluted from a paper chromatogram was investigated. This destruction is due to inpurities in the paper which contaminate the peptides. Prevention of such destruction can be achieved by predevelopment of the paper with 1 N NH4OH prior to paper chromatography.

Photochemical Yields in Ribonuclease and Oxidized Glutathione Irradiated at Different Wavelengths in the Ultraviolet

The quantum yields for the disruption of various amino acids in glutathione and ribonuclease by 229, 254, 265, and 280 nm UV photons have been determined. The results of the measurements on the destruction of tyrosine and histidine and the loss of enzymic function in RNAse and the disruption of cystine in both compounds lead to the following conclusions: (a) The photodestruction of some and perhaps many constituent amino acid residues does not cause RNAse inactivation. (b) Contrary to the basic premise of proposals made by other authors, the photochemical yields of constituent residues in a protein are not the same as that for the same amino acids in solution alone-the difference is a function of the exciting wavelength. Further, the extent of histidine destruction varies by a large factor among three proteins. (c) Consistent with previous predictions, the present results show that photons absorbed in the aromatic residues of RNAse cause the disruption of cystines elsewhere in the enzyme. (d) Although cystine disruption appears to be the most prevalent mode of RNAse inactivation by photons of the four wavelengths studied, some of the minor mechanisms leading to loss of enzymic function may vary with the UV energy.

Observations on the synthesis and destruction of tyrosine by Streptococcus faecalis R

Streptococcus faecalis R when grown in a double-strength medium rendered the medium deficient in folic acid and tyrosine. The organism was found to be capable of removing approximately ten times as much folic acid from the medium during the 24-hr. incubation period as it requires for maximum growth. Although Streptococcus faecalis R achieved maximum growth in the absence of added tyrosine if pyridoxal was present in the medium, the growth response obtained in the presence of tyrosine was proportional to the amount of tyrosine added at concentrations of tyrosine greater than 10 μ./10 ml. medium. Growth of S. faecalis R in the presence but not in the absence of pyridoxal caused a tyrosine deficiency to develop in the double-strength medium.