Turkey ovomucoid third domain inhibits eight different serine proteinases of varied specificity on the same ...Leu18-Glu19... reactive site

Biochemistry ◽  
1985 ◽  
Vol 24 (20) ◽  
pp. 5313-5320 ◽  
Author(s):  
Wojciech Ardelt ◽  
Michael Laskowski
Keyword(s):  
Serine Proteinases ◽  
Reactive Site ◽  
Ovomucoid Third Domain

Assignment of the13C-nmr spectra of virgin and reactive-site modified turkey ovomucoid third domain

Biopolymers ◽  
1990 ◽  
Vol 29 (2) ◽  
pp. 461-467 ◽  
Author(s):  
A. D. Robertson ◽  
G. I. Rhyu ◽  
W. M. Westler ◽  
J. L. Markley
Keyword(s):  
Nmr Spectra ◽  
Reactive Site ◽  
Ovomucoid Third Domain

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

scholarly journals Squash inhibitor family of serine proteinases.

1996 ◽  
Vol 43 (3) ◽  
pp. 431-444 ◽  
Author(s):  
J Otlewski ◽  
D Krowarsch
Keyword(s):  
Amino Acid ◽  
Growth Factor ◽  
Transforming Growth Factor Beta ◽  
Transforming Growth Factor ◽  
Cathepsin G ◽  
Structural Motif ◽  
Serine Proteinases ◽  
Reactive Site ◽  
Clotting Factors ◽  
Small Proteins

Squash inhibitors of serine proteinases form an uniform family of small proteins. They are built of 27-33 amino-acid residues and cross-linked with three disulfide bridges. The reactive site peptide bond (P1-P1') is between residue 5 (Lys, Arg or Leu) and 6 (always Ile). High resolution X-ray structures are available for two squash inhibitors complexed with trypsin. NMR solution structures have also been determined for free inhibitors. The major structural motif is a distorted, triple-stranded antiparallel beta-sheet. A similar folding motif has been recently found in a number of proteins, including: conotoxins from fish-hunting snails, carboxypeptidase inhibitor from potato, kalata B1 polypeptide, and in some growth factors (e.g. nerve growth factor, transforming growth factor beta 2, platelet-derived growth factor). Squash inhibitors are highly stable and rigid proteins. They inhibit a number of serine proteinases: trypsin, plasmin, kallikrein, blood clotting factors: Xa and XIIa, cathepsin G. The inhibition spectrum can be much broadened if specific amino-acid substitutions are introduced, especially at residues which contact proteinase. Squash inhibitors inhibit proteinases via the standard mechanism. According to the mechanism, inhibitors are substrates which exibit at neutral pH a high kcat/K(m) index for hydrolysis and resynthesis of the reactive site, and a low value of the hydrolysis constant.

Increasing the hydrolysis constant of the reactive site upon introduction of an engineered Cys14 Cys39 bond into the ovomucoid third domain from silver pheasant

2011 ◽  
Vol 17 (8) ◽  
pp. 595-600
Author(s):  
Hikaru Hemmi ◽  
Takashi Kumazaki ◽  
Shuichi Kojima ◽  
Takuya Yoshida ◽  
Tadayasu Ohkubo ◽  
...  
Keyword(s):  
Reactive Site ◽  
Hydrolysis Constant ◽  
Ovomucoid Third Domain

Solvent-assisted osmium staining of butyl acrylate and ethylene-propylene-diene in a styrene acrylonitrile matrix

1993 ◽  
Vol 51 ◽  
pp. 900-901 ◽  
Author(s):  
Gudrun A. Hutchins
Keyword(s):  
Butyl Acrylate ◽  
Room Temperature ◽  
Osmium Tetroxide ◽  
Staining Procedure ◽  
Reactive Site ◽  
Ethylene Propylene ◽  
Minimal Distortion ◽  
Styrene Acrylonitrile ◽  
Engineering Polymers ◽  
Effective Reaction

In order to optimize the toughening effect of elastomers in engineering polymers, it is necessary to characterize the size, morphology and dispersion of the specific elastomer within the polymer matrix. For unsaturated elastomers such as butadiene or isoprene, staining with osmium tetroxide is a well established procedure. The residual carbon-carbon double bond in these materials is the reactive site and forms a 1,2-dilato complex with the OsO4. Incorporation of osmium tetroxide into the elastomer not only produces sufficient contrast for TEM, but also crosslinks the elastomer sufficiently so that ultramicrotomy can be accomplished at room temperature with minimal distortion.Blends containing saturated elastomers such as butyl acrylate (BA) and ethylene propylene diene monomer (EPDM) cannot be stained directly with OsO4 because effective reaction sites such as C=C or -NH2 are not available in sufficient number. If additional reaction sites can be introduced selectively into the elastomer by a chemical reaction or the absorption of a solvent, a modified, two-step osmium staining procedure is possible.

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