A method for the direct detection of aromatic amino acid decarboxylase in electrophoretic media.
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Biomedical subjects
Publications and source records attributed to M Landon.
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The activity of gamma-glutamyltransferase was measured in a series of human breast milk samples collected during the first post natal week. All the samples showed considerable gamma-glutamyltransferase activity. The mean level fell from 28.8 U/ml to 3.9 U/ml seven days later. There was a highly significant correlation between gamma-glutamyltransferase and the protein content of the samples studied.
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A tentative but almost complete amino acid sequence for the subunit peptide chain of bovine liver glutamate dehydrogenase indicates a minimal size of 506 residues with a molecular weight of 56,100, in accord with the physical size of the subunit of 55,900. Inactivation with pyridoxal 5'-phosphate, followed by reduction with sodium borohydride, has permitted identification of the essential lysine as residue 97. Nitration of tyrosine-412 is accompanied by loss of the allosteric inhibitory effect of guanosine triphosphate. Comparison of the sequences of glutamate dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase has indicated that only two 12-residue sequences are similar in the two enzymes; this sequence includes reactive lysine-97 of the former enzyme.
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