Interscaffolding Additivity. Association of P1Variants of Eglin c and of Turkey Ovomucoid Third Domain with Serine Proteinases†

Biochemistry ◽  
1997 ◽  
Vol 36 (7) ◽  
pp. 1598-1607 ◽  
Author(s):  
M. A. Qasim ◽  
Philip J. Ganz ◽  
Charles W. Saunders ◽  
Katherine S. Bateman ◽  
Michael N. G. James ◽  
...  
Keyword(s):  
Serine Proteinases ◽  
Ovomucoid Third Domain ◽  
Eglin C

Binding of kunitz and eglin c inhibitors to serine proteinases: thermodynamic, kinetic and molecular aspects

1988 ◽  
Vol 47 (2-3) ◽  
pp. 297-306 ◽  
Author(s):  
Paolo Ascenzi ◽  
Gino Amiconi ◽  
Martino Bolognesi ◽  
Enea Menegatti ◽  
Mario Guarneri
Keyword(s):  
Serine Proteinases ◽  
Eglin C ◽  
Molecular Aspects

Despite Having a Common P1Leu, Eglin C Inhibits α-Lytic Proteinase a Million-fold More Strongly than Does Turkey Ovomucoid Third Domain†

Biochemistry ◽  
2006 ◽  
Vol 45 (38) ◽  
pp. 11342-11348 ◽  
Author(s):  
M. A. Qasim ◽  
Robert L. Van Etten ◽  
Tina Yeh ◽  
C. Saunders ◽  
P. J. Ganz ◽  
...  
Keyword(s):  
Ovomucoid Third Domain ◽  
Eglin C ◽  
Proteinase A

Serine proteinases in human cutaneous mastocytosis

1986 ◽  
Vol 278 (5) ◽  
pp. 363-366 ◽  
Author(s):  
J. E. Fr�ki ◽  
N. M. Schechter ◽  
G. S. Lazarus
Keyword(s):  
Serine Proteinases ◽  
Cutaneous Mastocytosis

Crystal and molecular structure of the bovine α-chymotrypsin-eglin c complex at 2.0 Å resolution

1992 ◽  
Vol 225 (1) ◽  
pp. 107-123 ◽  
Author(s):  
Francesco Frigerio ◽  
Alessandro Coda ◽  
Luisa Pugliese ◽  
Claudia Lionetti ◽  
Enea Menegatti ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Crystal And Molecular Structure ◽  
Eglin C ◽  
C Complex

Distribution of the granulocyte serine proteinases proteinase 3 and elastase in human glomerulonephritis

1995 ◽  
Vol 25 (2) ◽  
pp. 253-261 ◽  
Author(s):  
Christian Mrowka ◽  
Elena Csernok ◽  
Wolfgang L. Gross ◽  
Helmut E. Feucht ◽  
Ulrike Bechtel ◽  
...  
Keyword(s):  
Proteinase 3 ◽  
Serine Proteinases

scholarly journals Mouse macrophage elastase. Purification and characterization as a metalloproteinase

1981 ◽  
Vol 193 (2) ◽  
pp. 589-605 ◽  
Author(s):  
M J Banda ◽  
Z Werb
Keyword(s):  
Culture Medium ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Serine Proteinase ◽  
Peritoneal Macrophages ◽  
Serine Proteinases ◽  
Endogenous Inhibitor ◽  
Purification And Characterization ◽  
Predominant Form ◽  
Mouse Peritoneal Macrophages

Macrophage elastase was purified from tissue-culture medium conditioned by inflammatory mouse peritoneal macrophages. Characterized as a secreted neutral metalloproteinase, this enzyme was shown to be catalytically and immunochemically distinct from the mouse pancreatic and mouse granulocyte elastases, both of which are serine proteinases. Inhibition profiles, production of nascent N-terminal leucine residues and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of degraded elastin indicated that macrophage elastase is an endopeptidase, with properties of a metalloproteinase, rather than a serine proteinase. Macrophage elastase was inhibited by alpha 2-macroglobulin, but not by alpha 1-proteinase inhibitor. Macrophage elastase was resolved into three chromatographically distinct forms. The predominant form had mol.wt. 22 000 and was purified 4100-fold. Purification of biosynthetically radiolabelled elastase indicated that this form represented less than 0.5% of the secreted protein of macrophages. Approx. 800% of the starting activity was recovered after purification. Evidence was obtained for an excess of an endogenous inhibitor masking more than 80% of the secreted activity.

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