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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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The Role of Scaffolding in Standard Mechanism Serine Proteinase Inhibitors
Protein & Peptide Letters, 2005In single domain, "standard mechanism" protein inhibitors of serine proteinases, about a dozen residues make contact with the cognate enzyme. The remainder of the molecule, the scaffolding, holds the reactive site region of the inhibitor in a canonical conformation, improves the binding by about six orders of magnitude and protects it from proteolysis.
Clyde A, Kelly +2 more
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Serine proteinase inhibitors in the Compositae: distribution, polymorphism and properties
Phytochemistry, 2002Multiple molecular forms of inhibitors of trypsin (TI) and chymotrypsin (CI), which are typical digestive enzymes of insects, mammals and micro-organisms, and subtilisin (SI), a proteinase of many bacteria and phytopathogenic fungi, were identified in seeds and vegetative organs of the majority of 128 wild and cultivated species representing 65 genera ...
Alexander V, Konarev +6 more
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Structure and function of invertebrate Kazal-type serine proteinase inhibitors
Developmental & Comparative Immunology, 2010Proteinases and proteinase inhibitors are involved in several biological and physiological processes in all multicellular organisms. The proteinase inhibitors function as modulators for controlling the extent of deleterious proteinase activity. The Kazal-type proteinase inhibitors (KPIs) in family I1 are among the well-known families of proteinase ...
Vichien, Rimphanitchayakit +1 more
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Serine Proteinase Inhibitors from Vipera ammodytes Venom
European Journal of Biochemistry, 1983Three protein inhibitors of serine proteinases were isolated from the crude venom of the long‐nosed viper Vipera ammodytes ammodytes by ion‐exchange and gel chromatography. Two of them strongly inhibit trypsin (Ki= 3.4 × 10−10 and 5.6 × 10‐10 M), while the third one primarily inhibits chymotrypsin (Ki= 4.3 × 10‐9 M).
A, Ritonja, V, Turk, F, Gubensek
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A serine proteinase inhibitor from frog eggs with bacteriostatic activity
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2008By Sephadex G-50 gel filtration, Resource Q anionic exchange and C4 reversed phase liquid high performance liquid chromatography, a proteinase inhibitor protein (Ranaserpin) was identified and purified from the eggs of the odour frog, Rana grahami. The protein displayed a single band adjacent to the molecular weight marker of 14.4 kDa analyzed by SDS ...
Yaoping, Han +5 more
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Identification and characterization of serine proteinase inhibitors from Neospora caninum
Molecular and Biochemical Parasitology, 2004Two cDNA clones obtained from the Neospora caninum Expressed Sequence Tag project were selected by their homology with the Toxoplasma gondii serine proteinase inhibitor (serpin) gene, TgPI-1 and TgPI-2. One of them, named NcPI-H, showed several premature stop codons.
Susana, Bruno +6 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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DIFFERENTIAL INHIBITION OF SERINE PROTEINASES BY RABBIT α 1‐PROTEINASE INHIBITORS F AND S
International Journal of Peptide and Protein Research, 1981Inhibition of six serine proteinases (bovine trypsin and chymotrypsin, equine leucocyte proteinases type 1 and 2A, porcine pancreatic elastase type III and rabbit plasmin) by rabbit α1‐proteinase inhibitors F and S was studied. In each case examined, the F form reacted more rapidly.The number of moles of an enzyme inhibited by one mole of α1 ...
A, Koj, E, Regoeczi
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Biochemical and Biophysical Research Communications, 1997
The interaction of a bioengineered serpin (LEX032) with human leukocyte proteinase 3 (PR 3) has been investigated. LEX032 was found to be a time-dependent inhibitor of PR 3, forming a highly-stable enzyme-inhibitor complex (Ki 12 nM).
Groutas, William C. +4 more
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The interaction of a bioengineered serpin (LEX032) with human leukocyte proteinase 3 (PR 3) has been investigated. LEX032 was found to be a time-dependent inhibitor of PR 3, forming a highly-stable enzyme-inhibitor complex (Ki 12 nM).
Groutas, William C. +4 more
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