Results 191 to 200 of about 16,013 (203)
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[The role of serine endopeptidase in cucumber leaf senescence].
Zhi wu sheng li yu fen zi sheng wu xue xue bao = Journal of plant physiology and molecular biology, 2009The role of serine endopeptidase in cucumber leaf senescence was studied by using the inhibitor of serine endopeptidase and plant growth regulators (6-BA and ABA) on darkness-induced cucumber leaves. The results showed that the senescence of cucumber leaves were delayed by AEBSF [4-(2-aminoethyl) benzenesulfonyl fluoride hydrochloride], an inhibitor of
Peng, Zhang +4 more
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Serine Endopeptidase Activities of Cowpea Seeds: A Time Course during Development and Germination
Crop Science, 2019ABSTRACTProteases in plants carry out an essential role in protein turnover during seed development and germination. Cysteine proteases (EC 3.4.22) are well‐known participants of such processes. Serine proteases (EC 3.4.21), however, are far less reported as protagonists during these events.
Nathália B. Lima +6 more
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Phytochemistry, 2001
An endopeptidase was purified and characterized from green leaves of cucumber (Cucumis sativus L. suyo). The purified enzyme, a basic amino acid-specific endopeptidase with a pI of 5.0, was a monomeric protein of 80 kDa whose pH optimum was 9.5. Inhibitor analysis suggested that it was a serine endopeptidase and contained sulfhydryl groups essential ...
Y, Yamauchi +4 more
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An endopeptidase was purified and characterized from green leaves of cucumber (Cucumis sativus L. suyo). The purified enzyme, a basic amino acid-specific endopeptidase with a pI of 5.0, was a monomeric protein of 80 kDa whose pH optimum was 9.5. Inhibitor analysis suggested that it was a serine endopeptidase and contained sulfhydryl groups essential ...
Y, Yamauchi +4 more
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Canadian Journal of Microbiology, 2002
A keratinolytic Xanthomonas maltophilia strain (POA-1), cultured on feather meal broth, using keratin as its sole source of carbon and nitrogen, secretes several extracellular peptidases. The major serine peptidase was purified to homogeneity by a five-step procedure. Its purity was evaluated by capillary zone electrophoresis.
C H, De Toni +4 more
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A keratinolytic Xanthomonas maltophilia strain (POA-1), cultured on feather meal broth, using keratin as its sole source of carbon and nitrogen, secretes several extracellular peptidases. The major serine peptidase was purified to homogeneity by a five-step procedure. Its purity was evaluated by capillary zone electrophoresis.
C H, De Toni +4 more
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Biological Chemistry Hoppe-Seyler, 1992
Prolyl endopeptidase and dipeptidyl peptidase IV are serine proteases which cleave the peptide bonds at the carboxy group of proline residues. They do not show amino acid sequence homology with the known serine enzymes, but a possible relationship between them has not yet been examined.
L, Polgár, E, Szabo
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Prolyl endopeptidase and dipeptidyl peptidase IV are serine proteases which cleave the peptide bonds at the carboxy group of proline residues. They do not show amino acid sequence homology with the known serine enzymes, but a possible relationship between them has not yet been examined.
L, Polgár, E, Szabo
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Immunopharmacology, 1999
We have previously described a kinin-inactivating endopeptidase (H2), which was purified 19-fold from human urine by DEAE-cellulose chromatography and gel filtration. The enzyme was inhibited 100% by PMSF, TPCK and pOHMB. In the present communication, we further characterized this enzyme using the fluorogenic substrates Abz-RPPGFSPFRQ-EDDnp (Abz-BKQ ...
Quinto, BMR +5 more
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We have previously described a kinin-inactivating endopeptidase (H2), which was purified 19-fold from human urine by DEAE-cellulose chromatography and gel filtration. The enzyme was inhibited 100% by PMSF, TPCK and pOHMB. In the present communication, we further characterized this enzyme using the fluorogenic substrates Abz-RPPGFSPFRQ-EDDnp (Abz-BKQ ...
Quinto, BMR +5 more
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SEP-1 - a subtilisin-like serine endopeptidase from germinated seeds of Hordeum vulgare L. cv. Morex
Planta, 2002Proteolysis is crucial for all living cells. It regulates protein processing, intracellular protein levels and removes abnormal or damaged proteins from the cell, working as a cellular housekeeper. By means of proteolysis, cells can control the short-lived regulatory proteins that affect processes such as signal transduction and reception ...
FONTANINI, DEBORA, Jones B.L.
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Affinity and Specificity of Serine Endopeptidase-Protein Inhibitor Interactions
Journal of Molecular Biology, 1993Stanley Krystek +2 more
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