scholarly journals Reaction of azapeptides with chymotrypsin-like enzymes. New inhibitors and active site titrants for chymotrypsin A alpha, subtilisin BPN', subtilisin Carlsberg, and human leukocyte cathepsin G.

1984 ◽  
Vol 259 (7) ◽  
pp. 4279-4287
Author(s):  
B F Gupton ◽  
D L Carroll ◽  
P M Tuhy ◽  
C M Kam ◽  
J C Powers
Keyword(s):  
Active Site ◽  
Human Leukocyte ◽  
Cathepsin G ◽  
Subtilisin Carlsberg ◽  
Chymotrypsin A

Synthesis of 2-Phenylisothiazol-3(2H)-One 1,1-Dioxides: Inhibitors of Human Leukocyte Elastase

2003 ◽  
Vol 58 (1) ◽  
pp. 111-120 ◽  
Author(s):  
Michael Gütschow ◽  
Markus Pietsch ◽  
Kathleen Taubert ◽  
Tonia H. E. Freysoldt ◽  
Bärbel Schulze
Keyword(s):  
Active Site ◽  
Serine Proteases ◽  
Human Leukocyte ◽  
Cathepsin G ◽  
Time Dependent ◽  
Dependent Manner ◽  
Complex Type ◽  
Leukocyte Elastase ◽  
Human Leukocyte Elastase ◽  
Kinetic Investigations

Abstract A series of 2-phenylisothiazol-3(2H)-one 1,1-dioxides 14a - q were synthesized by oxidation of isothiazolium perchlorates 12. The inhibition of the serine proteases cathepsin G, chymotrypsin and human leukocyte elastase (HLE) by 14 was investigated. Some 4,5-diphenyl substituted derivatives ( 14i - k) were found to inhibit HLE in a time-dependent manner and exhibited kobs/[I] values > 500 M−1s−1. 14k (kobs/[I] = 2400 M−1s−1), was the most potent HLE inhibitor of this series. Kinetic investigations led to the conclusion that 2-phenylisothiazol-3(2H)-one 1,1-dioxides interact with HLE at the active site as well as at another binding site, resulting in a complex type of inhibition.

Mechanism-based inhibition of human leukocyte elastase and cathepsin G by susbtituted dihydrouracils

1994 ◽  
Vol 1227 (3) ◽  
pp. 130-136 ◽  
Author(s):  
William C. Groutas ◽  
Jeffrey B. Epp ◽  
Radhika Venkataraman ◽  
Jerald J. McClenaha ◽  
Fusao Tagusagawa
Keyword(s):  
Human Leukocyte ◽  
Cathepsin G ◽  
Leukocyte Elastase ◽  
Human Leukocyte Elastase

Inhibition of the human leukocyte endopeptidases elastase and cathepsin G and of porcine pancreatic elastase by N-oleoyl derivatives of heparin

1993 ◽  
Vol 46 (9) ◽  
pp. 1545-1549 ◽  
Author(s):  
Antonio Baici ◽  
Csaba Diczházi ◽  
András Neszmélyi ◽  
Elemér Móczár ◽  
William Hornebeck
Keyword(s):  
Human Leukocyte ◽  
Cathepsin G ◽  
Pancreatic Elastase ◽  
Porcine Pancreatic Elastase ◽  
Derivatives Of

Kinetic Studies on the Interaction of Eglincwith Human Leukocyte Elastase and Cathepsin G

1987 ◽  
Vol 368 (1) ◽  
pp. 299-308 ◽  
Author(s):  
Nancy J. BRAUN ◽  
Judith L. BODMER ◽  
G. Duke VIRCA ◽  
Gabrielle METZ-VIRCA ◽  
Reinhard MASCHLER ◽  
...  
Keyword(s):  
Human Leukocyte ◽  
Kinetic Studies ◽  
Cathepsin G ◽  
Leukocyte Elastase ◽  
Human Leukocyte Elastase

scholarly journals Action of human cathepsin G on the oxidized B chain of insulin

1977 ◽  
Vol 161 (1) ◽  
pp. 17-19 ◽  
Author(s):  
A M J Blow ◽  
A J Barrett
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Human Neutrophil ◽  
Cathepsin G ◽  
British Library ◽  
Neutral Proteinase ◽  
Terminal Residue ◽  
Human Cathepsin ◽  
Chymotrypsin A

The specificity of cathepsin G, a serine neutral proteinase from human neutrophil leucotyes, was determine dby its action on the insulin B chain. The most susceptible bonds were Phe-24-Phe-25, Leu-15-Tyr-16 and Tyr-16-Leu-17. Other bonds hydrolysed were Leu-6-Cys(O3H)-7, Leu-11-Val-12, Leu-17-Val-18 and Phe-25-Tyr-26. These results suggest that the specificity of cathespin G is closer to that of pig chymotrypsin C than ox Chymotrypsin A. Tables listing amino acid composition, N-terminal residue, and yields of isolated peptides have been deposited as Supplementary Publication SUP 50 075 (8 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7B2, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1977) 161,1.

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