Results 261 to 270 of about 71,530 (308)

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
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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
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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
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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
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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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Detection of serine proteinase inhibitors in human cornified cells

Biochemical and Biophysical Research Communications, 1981
Abstract A screening test for serine proteinase inhibitors revealed trypsin and urokinase inhibitors in the extract of human cornified cells. No inhibition for α-chymotrypsin, thrombin or plasmin was detected. Characterization of the inhibitors separated with a Sephacryl S-200 gel column demonstrated that: 1) trypsin inhibitor with a molecular weight
T, Hibino, S, Izaki, M, Izaki
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Inhibitor Complexes of the Pseudomonas Serine-Carboxyl Proteinase

Biochemistry, 2001
Crystal structures of the serine-carboxyl proteinase from Pseudomonas sp. 101 (PSCP), complexed with a number of inhibitors, have been solved and refined at high- to atomic-level resolution. All of these inhibitors (tyrostatin, pseudo-tyrostatin, AcIPF, AcIAF, and chymostatin, as well as previously studied iodotyrostatin and pseudo-iodotyrostatin) make
A, Wlodawer, M, Li, A, Gustchina, Z, Dauter, K, Uchida, H, Oyama, N E, Goldfarb, B M, Dunn, K, Oda   +8 more
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Chemoattractant activity of Staphylococcus aureus serine proteinase modified human plasma ?-1-proteinase inhibitor

Antonie van Leeuwenhoek, 1989
S. aureus serine proteinase inactivates human alpha-1-proteinase inhibitor (alpha-1-PI) by attacking a single peptide bond between Glu354 and Ala355 giving a modified inhibitor which is a tight complex of Mr = 4,000 and 48,000 fragments. In the present paper we show that this proteolytically inactivated alpha-1-PI is a potent chemotactic factor for ...
K, Baran, M, Górka, J, Potempa, Z, Porwit-Bóbr   +3 more
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Peptidic inhibitors of serine proteinases of plant origin

2013
Serine 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, Adam Lesner, Anna Łęgowska, Magdalena Wysocka   +3 more
  +4 more sources