Results 261 to 270 of about 37,649 (300)

Boophilus microplus tick larvae, a rich source of Kunitz type serine proteinase inhibitors [PDF]

open access: yesBiochimie, 2004
Serine proteinase inhibitors from Boophilus microplus tick larvae (BmTIs) were purified by affinity chromatography on a trypsin-Sepharose column. BmTIs presented molecular weight between M, 6200 and 18,400 and inhibitory activity for trypsin, HuPK (human
Sérgio D Sasaki   +2 more
exaly   +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   +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   +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   +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   +4 more
openaire   +2 more sources

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   +5 more
openaire   +2 more sources

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
openaire   +2 more sources

The Effect of a Serine Proteinase Inhibitor on DIC in Septic Abortion

Asia-Oceania Journal of Obstetrics and Gynaecology, 1987
AbstractA 21‐year‐old woman developed septic shock complicated by acute renal insufficiency after D & C to terminate early pregnancy.Although immediate and aggressive treatment improved the profound cardiovascular collapse, DIC became manifest.
S, Takeda   +7 more
openaire   +2 more sources

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   +2 more
openaire   +2 more sources

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   +8 more
openaire   +2 more sources

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