Comparison of Streptomyces griseus and bovine trypsin by active site analysis using fluorescent acyl groups-Reference-Cited by-同舟云学术

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Comparison of Streptomyces griseus and bovine trypsin by active site analysis using fluorescent acyl groups

Published:1987-07 Issue:3 Volume:913 Page:292-299
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Tanizawa Kazutaka,Nakano Michiharu,Kanaoka Yuichi

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference17 articles.

1. Proteolytic enzymes. 7. "Inverse substrates" for trypsin. Efficient enzymic hydrolysis of certain esters with a cationic center in the leaving group

2. Topographical analysis of trypsin active site structure by means of the “inverse substrate” method

3. Comparative Studies on the Structure of Active Sites. Behavior of “Inverse Substrates” toward Trypsin and Related Enzymes1

4. Enzymic and physicochemical properties of Streptomyces griseus trypsin

5. Amino acid sequence of Streptomyces griseus trypsin. Cyanogen bromide fragments and complete sequence

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