Results 311 to 320 of about 194,365 (341)
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Proteinase-Protein Inhibitor Interaction

Fibrinolysis, 1991
Until recently, the "substrate-like" "canonical" inhibition by the "small" serine proteinase inhibitors, and the product-like inhibition by the carboxypeptidase inhibitor, provided the only models for protein inhibitor-proteinase interactions. The recently published structures of cystatin/stefin-papain complexes and of hirudin-thrombin complexes reveal
Wolfram Bode, Robert Huber
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ChemInform Abstract: PROTEINASE INHIBITORS. 1. INHIBITORS OF ELASTASE

Chemischer Informationsdienst, 1977
Abstract36 Peptid‐carbazate werden in Tabellen aufgeführt und als Inhibitoren von Elastase geprüft z.B. Vertreter der Art (V) und (VI).
Shu Shu Yang   +6 more
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Acrosomal Proteinase and Proteinase Inhibitor of Human Spermatozoa

Science, 1972
The acrosomal proteinase of human spermatozoa was characterized and differs from other human proteinases. The enzyme has optimal activity at p H 8.0, is inactive below p H 5.0 or above p H 10.5, requires calcium for maximum activity, hydrolyzes fibrinogen, gelatin, and
L. J. D. Zaneveld   +2 more
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5 Inhibitors of HIV Proteinase

1995
Publisher Summary This chapter focuses on inhibitors of HIV Proteinase. X-ray crystallographic structures of HIV proteinase complexed with a diverse range of inhibitors have now been published. Despite large differences in the structures of the bound inhibitors, the structure of the enzyme is remarkably well conserved in all of the complexes.
Joseph Armstrong Martin   +2 more
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Proteinase and Proteinase Inhibitor Localization in the Human Placenta

International Journal of Gynecological Pathology, 1989
Standard immunoperoxidase techniques were used to investigate the distribution of the intracellular proteinase cathepsin D, two serine proteinase inhibitors--alpha 1-antitrypsin (alpha 1-AT) and alpha 1-antichymotrypsin (alpha 1-AChy)--and plasma fibrin stabilizing factor XIII (FXIII) in paraffin-embedded tissues from early and late intrauterine ...
Earl U   +3 more
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Proteinase inhibitors as antileishmanial agents

Transactions of the Royal Society of Tropical Medicine and Hygiene, 1982
Leishmania mexicana mexicana amastigote proteinase activity was largely inhibited by low concentrations of leupeptin, antipain and two epoxysuccinates, compounds known to affect cysteine proteinases. Of these inhibitors, only two had leishmanicidal activity. trans-Dicyclohexylepoxysuccinate at 10 microgram/ml inhibited the in vitro transformation of L.
J. Capaldo, D.T. Hart, Graham H. Coombs
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Proteinase Inhibitors and Proteinases of Human Semen

1974
During the First International Research Conference on Proteinase Inhibitors, a survey was presented concerning the proteinases of spermatozoa and seminal plasma as was known until that time [1, 2]. In summary, a proteinase from rabbit spermatozoa was purified and characterized, and shown to differ from other known pro-teolytic enzymes. It was given the
Gebhard F.B. Schumacher   +3 more
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Proteinase Inhibitors

1981
Publisher Summary This chapter discusses proteinase inhibitors. Proteinase inhibitors found in plants are typically polypeptides and proteins composed entirely of L-amino acids linked through peptide bonds. They generally contain high percentages of half-cystine residues, present as disulfide cross-links, and it is not uncommon for inhibitors to have ...
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Decompensation in proteinase-inhibitor system and application of proteinase inhibitors in pemphigus and pemphigoid

Journal of Dermatological Science, 1992
The goal of this study was to determine levels of serine proteinases and their inhibitors in serum and blister fluid of patients with pemphigus vulgaris (PV) and bullous pemphigoid (BP) in the course of treatment with prednisolone and proteinase inhibitors such as Contrycal and epsilon-aminocaproic acid.
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Plant Serine Proteinase Inhibitors

Protein & Peptide Letters, 2005
Evidence that establishes the mechanism of the classes of plant proteinase inhibitors (PIs) is evaluated. Of the eight classes of PIs, six are unique to plants. Except for plant serpins, there is evidence that PIs from all other classes form tight binding complexes with their target proteinases, and that they follow the standard mechanism of inhibition.
J.T. Christeller, William A. Laing
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