Yeast glyceraldehyde-3-phosphate dehydrogenase as a typical SH enzyme is inactivated by the antipodes of a-iodopropionic acid and its amide at different rates. The apoenzyme reacts faster with the D(+) antipode of the free a-iodopropionic acid (k D /k L = 6.8) and the L(-) antipode of the amide (k L /k D = 3). On addition of NAD + the stereoselectivity of the...
Proteolytic activity at neutral pH can be demonstrated in extracts from beef spleen. This activity is completely due to an aminopeptidase - or a number of aminopeptides - which is able to hydrolyse proteins completely to amino acids. No evidence was found for the presence of endopeptidases active at neutral pH. The enzyme resembles to some extent swine kidney aminopeptides.
By double-diffusion and immunoelectrophoresis, using rabbit anti-sweat protein immune serum, an alpha 2 -globulin component of glycoprotein character was found in sweat, saliva, tears, human milk, colostrum and cerumen.
The biosynthesis of purine deoxyribonucleotides was studied in the context of general purine nucleotide metabolism in the chick with the aid of radioactive nucleic acid precursors. Our results showed that in chick liver and intestine, the nucleoside phosphate reductase system so firmly established in E. coli  and L. leichmanni  is not exclusively responsible for the biosynthesis of purine deoxyribonucleotides.
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