Results 271 to 280 of about 37,649 (300)
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Molecular Reproduction and Development, 2007
AbstractWe have recently identified and characterized twoimplantationserineproteinase genes, ISP1 and ISP2, which give rise to a dimeric proteinase, ISP that facilitates embryo invasion during peri‐implantation period. As many proteinases have cognate serpins that regulate their proteolytic activity, we have been investigating anti‐tryptases, expressed
Navneet, Sharma +4 more
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AbstractWe have recently identified and characterized twoimplantationserineproteinase genes, ISP1 and ISP2, which give rise to a dimeric proteinase, ISP that facilitates embryo invasion during peri‐implantation period. As many proteinases have cognate serpins that regulate their proteolytic activity, we have been investigating anti‐tryptases, expressed
Navneet, Sharma +4 more
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Journal of Biochemistry, 2008
The 20S proteasome (20S) is an intracellular threonine proteinase (Mr 750,000) that plays important roles in many cellular regulations. Several synthetic peptide inhibitors and bacteria-derived inhibitors such as lactacystin and epoxomicin have been identified as potent proteasome inhibitors.
Kimihiko, Yabe, Takehiko, Koide
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The 20S proteasome (20S) is an intracellular threonine proteinase (Mr 750,000) that plays important roles in many cellular regulations. Several synthetic peptide inhibitors and bacteria-derived inhibitors such as lactacystin and epoxomicin have been identified as potent proteasome inhibitors.
Kimihiko, Yabe, Takehiko, Koide
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Protein Inhibitors of Serine Proteinases — Mechanism and Classification
1986Protein proteinase inhibitors are widely distributed in plants, animals and microorganisms. They can be conveniently grouped since most frequently they inhibit proteinases belonging only to a single mechanistic class. Protein inhibitors of serine proteinases have been most extensively studied.
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Peptidic inhibitors of serine proteinases of plant origin
2013Serine proteinases play important roles in many physiological processes and in consequence, when unbalanced, are responsible for numerous severe diseases. The most predominant mechanism of their control is the ubiquitous presence of their inhibitors.
Krzysztof Rolka +3 more
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Enzyme and Microbial Technology, 1992
Peptidyl chloromethyl ketones were used for the specific labeling of proteinases by attaching a biotin group to the N-terminal end of the peptide. Such labeled peptide inhibitors allowed the detection and quantitation of proteolytic enzymes immobilized on the plastic surface of a microtiter plate, as well as on nitrocellulose.
Breton-Maintier, C. +2 more
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Peptidyl chloromethyl ketones were used for the specific labeling of proteinases by attaching a biotin group to the N-terminal end of the peptide. Such labeled peptide inhibitors allowed the detection and quantitation of proteolytic enzymes immobilized on the plastic surface of a microtiter plate, as well as on nitrocellulose.
Breton-Maintier, C. +2 more
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Biochemistry (Moscow), 2004
The inhibition of exogenous serine proteinases of different origin by cationic protease inhibitors BWI-1c, -2c, -3c, and -4c from buckwheat (Fagopyrum esculentum Moench) seeds has been studied. High efficiency of the inhibitors in binding bovine trypsin and chymotrypsin as well as their broad antiprotease effect, including inhibition of proteinases ...
T A, Tsybina +4 more
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The inhibition of exogenous serine proteinases of different origin by cationic protease inhibitors BWI-1c, -2c, -3c, and -4c from buckwheat (Fagopyrum esculentum Moench) seeds has been studied. High efficiency of the inhibitors in binding bovine trypsin and chymotrypsin as well as their broad antiprotease effect, including inhibition of proteinases ...
T A, Tsybina +4 more
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Photo‐CIDNP study of interactions of serine proteinases with their protein inhibitors
Biopolymers, 1983AbstractPhotochemically induced dynamic nuclear polarization was used to study the accessibility of surface tyrosine and tryptophan residues in proteinases, in their protein inhibitors and in the proteinase–inhibitor complexes. The accessibility probe is the triplet of 10‐(carboxyethyl) flavin formed by optical excitation.
K A, Muszkat +3 more
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Serine proteinase inhibitor families in Rhipicephalus microplus [PDF]
, 2008 The search for Rhipicephalus (Boophilus) microplus (cattle tick) vaccine candidates is a high research priority in Australia. Serine proteinase inhibitors (serpins) are implicated as potential vaccine candidates due to their ability to interfere with ...
Kurscheid, S. +4 more
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Reversible Inhibitors of Serine Proteinases
1995Herbert R. Wenzel, Harald Tschesche
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