Results 151 to 160 of about 754,866 (196)

Serine proteinase inhibitors in arthropod immunity

Developmental and Comparative Immunology, 1999
Arthropod hemolymph contains proteins with serine proteinase inhibitory activity. These inhibitors may exist in plasma or in hemocyte granules. Serine proteinase inhibitors from the Kazal, Kunitz, alpha-macroglobulin, and serpin families have been identified in arthropod hemolymph and have been characterized biochemically.
Michael Kanost
exaly   +3 more sources

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.
John, Christeller, William, Laing
openaire   +2 more sources

Inhibition of Serine Proteinases by Squash Inhibitors

Biological Chemistry Hoppe-Seyler, 1990
The squash inhibitors of serine proteinases have been discovered as proteins, which inhibit the catalytic activity of bovine trypsin. In this report we show, that three human enzymes of trypsin-like specificity - i.e. plasmin, plasma kallikrein and thrombin - are also inhibited by squash inhibitors.
J, Otlewski, T, Zbyryt, I, Krokoszyńska, T, Wilusz   +3 more
openaire   +2 more sources

Prediction of new serine proteinase inhibitors

Nature Structural & Molecular Biology, 1994
We describe here the use of a rapid computational method to predict the relative binding strengths of a series of small-molecule ligands for the serine proteinase trypsin. Flexible molecular models of the ligands were docked to the proteinase using an all-atom potential set, without cutoff limits for the non-bonded and electrostatic energies.
I V, Kurinov, R W, Harrison
openaire   +2 more sources

The distribution of serine proteinase inhibitors in seeds of the Asteridae

Phytochemistry, 2004
The Asteridae is one of the most successful clades of flowering plants comprising some 80,000 species. Despite this diversity, analysis of seeds from 398 species (representing 8 orders, 32 families and 181 genera) showed just two major types of serine proteinase inhibitors (PI). PIs of the potato inhibitor I family were widely distributed.
Alexander V, Konarev, Jonathan, Griffin, Galina Yu, Konechnaya, Peter R, Shewry   +3 more
openaire   +2 more sources

SORGHUM PROTEINASE INHIBITORS

International Journal of Peptide and Protein Research, 1979
Investigations have been carried out on the complex formed between sorghum Inhibitor III and α‐chymotrypsin by physico‐chemical methods. An apparent dissociation constant (Ki) of 4.0 times 10‐8 M has been calculated for the complex. This enzyme‐inhibitor complex was isolated by gel filtration on Sephadex G‐75 and a molecular weight of 48,000 was ...
Kumar, Harish PM, Virupaksha, Tumkur K, Vithayathil, Paul Joseph   +2 more
openaire   +2 more sources

Serine Proteinase Inhibitors in the Skin: Role in Homeostasis and Disease

Current Protein & Peptide Science, 2005
Serine proteinases fulfill and facilitate a broad spectrum of biological processes. They are held in check by different specific inhibitors. This delicate balance can be disturbed by genetic defects or exogenous influences and has been shown as the underlying or promoting cause for a large number of different diseases.
Hans-Jürgen, Mägert, Katrin, Drögemüller, Michael, Raghunath   +2 more
openaire   +2 more sources

Cationic Inhibitors of Serine Proteinases from Buckwheat Seeds

Biochemistry (Moscow), 2001
Preparations of low molecular weight protein inhibitors of serine proteinases have been obtained from buckwheat (Fagopyrum esculentum) seeds by chromatography of seed extract on trypsin-Sepharose 4B, Mono-Q, and Mono-S ion exchangers (FPLC regime). Their molecular masses, determined by mass spectrometry, were 5203 (BWI-1c), 5347 (BWI-2c), 7760 (BWI-3c),
T A, Tsybina, Y E, Dunaevsky, A K, Musolyamov, T A, Egorov, M A, Belozersky   +4 more
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LEKTI: a multidomain serine proteinase inhibitor with pathophysiological relevance

The International Journal of Biochemistry & Cell Biology, 2002
Proteinase inhibitors are important negative regulators of proteinase action in vivo and are thus involved in several pathophysiological processes. Starting with the isolation of two new peptides from human blood filtrate, we succeeded in cloning a cDNA encoding the precursor protein for a novel 15-domain Kazal-type-related serine proteinase inhibitor.
Hans Jürgen, Mägert, Peter, Kreutzmann, Ludger, Ständker, Michael, Walden, Katrin, Drögemüller, Wolf Georg, Forssmann   +5 more
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The Role of Scaffolding in Standard Mechanism Serine Proteinase Inhibitors

Protein & Peptide Letters, 2005
In 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, Michael, Laskowski, M A, Qasim   +2 more
openaire   +2 more sources