نتایج جستجو برای: cysteine proteinases

تعداد نتایج: 36425  

Journal: :The Biochemical journal 1988
P Rauber B Walker S Stone E Shaw

Some sulphonium salts derived from lysine were synthesized with the general structure R-Lys-CH2S+-(alkyl)2. They were examined as inhibitors of the cysteine proteinase clostripain, which has a preference for cleaving peptide bonds at the carboxy group of basic amino acids, and of a number of trypsin-related serine proteinases. Clostripain was irreversibly inactivated by all reagents examined, b...

Journal: :Plant physiology 1992
R Wrobel B L Jones

Barley endoproteolytic enzymes are important to germination because they hydrolyze endosperm storage proteins to provide precursors for new protein synthesis. We recently developed an electrophoretic method utilizing gel-incorporated protein substrates to study the endoproteinases of 4-d-germinated barley (Hordeum vulgare L. cv Morex) grain. This work extends those findings to determine the tem...

Journal: :Biochemical Society transactions 1989
D Wilcox R W Mason

NADH could not be freeze-stored at -25°C in 50 mMsodium phosphate buffer (pH range 6-8 20°C) without serious loss of the nucleotide; however, no losses were seen upon freeze storage in 50 mM-Hepes buffer (pH range 7-8, 20°C). The rate of NADH degradation was greater (approx. 2-fold) in 50 mMthan in 5 mM-sodium phosphate buffer, although NADH values at both buffer concentrations were similar (5%...

Journal: :Journal of cell science 1995
K Fuller T J Chambers

Osteoclasts resorb the extracellular matrix of bone by secreting protons and enzymes into a circumpherentially sealed compartment between the osteoclast and the bone surface. Although the lysosomal cysteine proteinases play a major role in matrix degradation by osteoclasts, collagenase (matrix metalloproteinase-1, EC 3.4.24.7) is also required for osteoclastic bone resorption, and may be direct...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1984
K A Kozlowski F H Wezeman R M Schultz

The fluorescent proteinase transition-state analog inhibitor, dansyl-L-argininal (DnsArgH), may be a selective probe of cysteine and serine-type proteinases in a fibrosarcoma tumor cell line (HSDM1C1). DnsArgH binds with high affinity to proteinases because of its transition-state analog properties, and on association it gives a dramatically increased fluorescent yield. The DnsArgH binding is i...

Journal: :The Journal of clinical investigation 1993
S Reed J Bouvier A S Pollack J C Engel M Brown K Hirata X Que A Eakin P Hagblom F Gillin

Cysteine proteinases are hypothesized to be important virulence factors of Entamoeba histolytica, the causative agent of amebic dysentery and liver abscesses. The release of a histolytic cysteine proteinase from E. histolytica correlates with the pathogenicity of both axenic strains and recent clinical isolates as determined by clinical history of invasive disease, zymodeme analysis, and cytopa...

Journal: :Biology bulletin of the Russian Academy of Sciences 2021

Abstract— The expression of the genes encoding inhibitors serine ( ISP ) and cysteine ​​proteinases ICP was studied in roots tomato plants resistant susceptible to root-knot nematode Meloidogyne incognita during infection under effects signaling molecules: salicylic (SA) jasmonic (JA) acids. It shown that, upon infection, are characterized by an increased accumulation transcripts at stages pene...

2016
Gillian Stepek Ann E. Lowe David J. Buttle Ian R. Duce Jerzy M. Behnke

Infectionswith gastrointestinal (GI) nematodes are amongst themost prevalent worldwide, especially in tropical climates. Control of these infections is primarily through treatment with anthelmintic drugs, but the rapid development of resistance to all the currently available classes of anthelmintic means that alternative treatments are urgently required. Cysteine proteinases from plants such as...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید