Showing papers by "Alexander N. Glazer published in 1967"

TL;DR: Data suggest that the enzyme requires a nonprotonated imidazole group for activity, and the subtilisins thus resemble trypsin and chymotrypsin with respect to the relative rates of cleavage of ester and amide substrates.

TL;DR: It was found that papaya lysozyme has a molecular weight of about 25,000 and that glycine is its sole amino-terminal residue, and molecular weight determinations in dissociating solvents indicate that the molecule consists of a single polypeptide chain.

TL;DR: The flagellins of Bacillus subtilis strain 19 and Spirillum serpens have been characterized by physical, chemical and immunochemical methods and contain a single type of protein subunit of molecular weight approximately 40,000.

TL;DR: Determination of the complete amino acid sequence of wheat germ cytochrome c has shown that the molecule consists of a single polypeptide chain of 112 residues, on alignment with mammalian cytochromes.

TL;DR: In this article, the binding site for the dye Biebrich Scarlet overlaps the active site region in α-chymotrypsin, and showed no significant spectral perturbation in the presence of these proteins, under the conditions used in this study.

TL;DR: Thionine to chymotrypsin is not affected by substrates, inhibitors, or chemically reactive substrate analogues; hence, the thionine-binding site in chymotsin does not appear to include any part of the active site region.