The Specific Binding of Biebrich Scarlet to the Active Site of α-Chymotrypsin
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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.About:
This article is published in Journal of Biological Chemistry.The article was published on 1967-10-10 and is currently open access. It has received 32 citations till now. The article focuses on the topics: Biebrich scarlet & Active site.read more
Citations
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Journal ArticleDOI
Subtilisin Carlsberg. V. The complete sequence; comparison with subtilisin BPN'; evolutionary relationships.
TL;DR: Within the subtilisins, there are a number of distinct repetitions of sequence; this suggests that the proteins may have evolved from shorter peptide chains by some process of extension of the sequence.
Book ChapterDOI
16 Subtilisins: Primary Structure, Chemical and Physical Properties
TL;DR: The sequence of subtilisin BPN' was deduced from studies of the tryptic, chymotryptic, peptic, and cyanogen bromide digests, and there is no apparent homology with the sequences of the pancreatic proteinases.
Journal ArticleDOI
Interaction of Cibacron Blue 3G-A and related dyes with nucleotide-requiring enzymes.
TL;DR: Inhibition studies indicate that the portion of the dye molecule necessary for effective inhibition of nucleotide binding is a structure similar to 1-amino-4(4′-aminophenylamino)-anthraquinone-2,3′-disulfonic acid (ASSO; III).
Journal ArticleDOI
Purification, characterization, and properties of an aryl aldehyde oxidoreductase from Nocardia sp. strain NRRL 5646.
Tao Li,John P. N. Rosazza +1 more
TL;DR: An aryl aldehyde oxidoreductase from Nocardia sp.
References
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Measurement of protein-binding phenomena by gel filtration.
J.P. Hummel,William J. Dreyer +1 more
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Sulfonyl Fluorides as Inhibitors of Esterases. I. Rates of Reaction with Acetylcholinesterase, α-Chymotrypsin, and Trypsin
David Fahrney,Allen M. Gold +1 more
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