Results 211 to 220 of about 265,113 (235)
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A novel leupeptin-sensitive serine endopeptidase present in normal and malignant rat mammary tissues
Molecular and Cellular Biochemistry, 1990N-Methyl-N-nitrosourea (MNU)-induced rat mammary adenocarcinomas contain high levels of a novel leupeptin-sensitive serine endopeptidase. Its properties apparently differ from those of other similar endopeptidases reported to be present in various normal and malignant mammalian tissues. The same leupeptinsensitive serine endopeptidase was also detected
Isao Eto
exaly +3 more sources
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 ...
D. Fontanini, B. Jones
semanticscholar +3 more sources
Classification of sheep abomasal mucosal mast cell proteinase as a serine endopeptidase (EC 3.4.21).
International Journal of Biochemistry, 19881. Diisopropylphosphofluoridate (Dip-F) and phenylmethanesulphonylfluoride (Pms-F) are inhibitors of "serine" proteinases, and L-trans-epoxysuccinylleucylamido-(4-guanido)-butane (E-64) is an inhibitor of "thiol" proteinases. The effects of these inhibitors on sheep mast cell proteinase (SMCP) were examined. 2.
D. Knox, J. Huntley
semanticscholar +3 more sources
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 Polgar
exaly +3 more sources
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 Polgar
exaly +3 more sources
Serine Endopeptidase Allergens from Dermatophagoides Species
, 2013T. Takai
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Characterization of Serine Endopeptidases in Cotyledons of Germinated Vigna mungo Seeds
Journal of Plant Research, 1999seeds. SEP activity was separated into two isoforms by CM-cellulose column chromatography. These forms, termed SEP-1 and SEP-II, showed endopeptidase activities even at acidic pH, suggesting that SEPs are unique serine endopeptidases, since most serine proteases are optimum at neutral pH.
Tomoki Hosokawa +2 more
openaire +1 more source
Journal of Agricultural and Food Chemistry, 2022
Soy sauce secondary precipitate formed due to the B3 subunit seriously affects soy sauce's appearance quality. In this study, a prolyl endopeptidase (APE) from Aspergillus niger, which could degrade approximately 50% of the B3 subunit and increase ...
Pei Shan +9 more
semanticscholar +1 more source
Soy sauce secondary precipitate formed due to the B3 subunit seriously affects soy sauce's appearance quality. In this study, a prolyl endopeptidase (APE) from Aspergillus niger, which could degrade approximately 50% of the B3 subunit and increase ...
Pei Shan +9 more
semanticscholar +1 more source
Comparative characterization of two serine endopeptidases from Nocardiopsis sp. NCIM 5124
Biochimica et Biophysica Acta (BBA) - General Subjects, 2000A protease-producing, crude oil degrading marine isolate was identified as Nocardiopsis sp. on the basis of the morphology, cell wall composition, mycolic acid analysis and DNA base composition. The Nocardiopsis produces two extracellular proteases, both of which are alkaline serine endopeptidases.
V S, Dixit, A, Pant
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