Self Purification of Two Serine Endopeptidases [PDF]
Proceedings of the National Academy of Sciences, 1972 We have reported that a serine protease from Pronase, homologous with bovine chymotrypsin, is both active and stable in 6 M guanidinium chloride. The present investigation examined the possibility that this unique property might be used to permit the enzyme to engage in its own purification by cleaving companion proteins to low-molecular ...
William M. Awad +2 more
core +6 more sources
Genetic Biodiversity and Posttranslational Modifications of Protease Serine Endopeptidase in Different Strains of Sordaria fimicola [PDF]
BioMed Research International, 2023 Genetic variations (mutation, crossing over, and recombination) act as a source for the gradual alternation in phenotype along a geographic transect where the environment changes. Posttranslational modifications (PTMs) predicted modifications successfully in different and the same species of living organisms.
Uzma Naureen +5 more
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Homologous inhibitors from potato tubers of serine endopeptidases and metallocarboxypeptidases. [PDF]
Proceedings of the National Academy of Sciences, 1976 A potent polypeptide inhibitor of chymotrypsin has been purified from Russett Burbank potatoes. The inhibitor has no effect on bovine carboxypeptidases A or B but exhibits homology with a carboxypeptidase inhibitor that is also present in potato tubers.
Claus HASS +2 more
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Purification and biochemical characterization of a vacuolar serine endopeptidase induced by glucose starvation in maize roots [PDF]
Biochemical Journal, 1996 An endopeptidase (designated RSIP, for root-starvation-induced protease) was purified to homogeneity from glucose-starved maize roots. The molecular mass of the enzyme was 59 kDa by SDS/PAGE under reducing conditions and 62 kDa by gel filtration on a Sephacryl S-200 column. The isoelectric point of RSIP was 4.55. The purified enzyme was stable, with no
Franck JAMES +4 more
+7 more sources
Substrate Specificity of Honeydew Melon Protease D, a Plant Serine Endopeptidase [PDF]
Bioscience, Biotechnology, and Biochemistry, 1997 The substrate specificity of honeydew melon (Cucumis melo var. inodorus Naud) protease D was studied by the use of synthetic substrates and oligopeptides derived from a protein hydrolyzate. The hydrolysis rates of succinyl-(L-Ala)1-3-p-nitroanilide (Suc-(Ala)1-3-pNA) the hydrolysis rate progressively rose in proportion to the increased chain length ...
Hiroo Yonezawa +2 more
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Insights into the efficient degradation mechanism of extracellular proteases mediated by Purpureocillium lilacinum [PDF]
Frontiers in MicrobiologyProtease secretion is crucial for degrading nematode cuticles using nematophagous fungus Purpureocillium lilacinum, but the secretion pattern of protease remains poorly understood.
Xiujun Zhang +7 more
doaj +2 more sources
Specific fluorogenic substrates for neprilysin (neutral endopeptidase, EC 3.4.24.11) which are highly resistant to serine- and metalloproteases [PDF]
Brazilian Journal of Medical and Biological Research, 1997 Two intramolecularly quenched fluorogenic peptides containing o-aminobenzoyl (Abz) and ethylenediamine 2,4-dinitrophenyl (EDDnp) groups at amino- and carboxyl-terminal amino acid residues, Abz-DArg-Arg-Leu-EDDnp (Abz-DRRL-EDDnp) and Abz-DArg-Arg-Phe-EDDnp (Abz-DRRF-EDDnp), were selectively hydrolyzed by neutral endopeptidase (NEP, enkephalinase ...
Marco Alberto Medeiros +4 more
openalex +9 more sources
Prolyl Endopeptidase-Like Facilitates the α-Synuclein Aggregation Seeding, and This Effect Is Reverted by Serine Peptidase Inhibitor PMSF [PDF]
Biomolecules, 2020 The aggregation of α-synuclein (α-Syn) is a characteristic of Parkinson’s disease (PD). α-Syn oligomerization/aggregation is accelerated by the serine peptidase, prolyl oligopeptidase (POP). Factors that affect POP conformation, including most of its inhibitors and an impairing mutation in its active site, influence the acceleration of α-Syn ...
Gabriel S. Santos +4 more
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Action of serine carboxypeptidases on endopeptidase substrates, peptide‐4‐methyl‐coumaryl‐7‐amides [PDF]
European Journal of Biochemistry, 1985 Carboxypeptidase Y hydrolyzed N‐substituted peptide‐4‐methylcoumarin‐7‐amides (peptide‐NH‐Mec) at pH 7 by releasing 7‐amino‐4‐methylcoumarin (NH2‐Mec) which was then followed by carboxypeptidase action. In particular, a chymotrypsin‐directed substrate, Suc‐Leu‐Leu‐Val‐Tyr‐NH‐Mec, was hydrolyzed by the enzyme with a second‐order rate constant of 7200 ...
Shigeru Kunugi +2 more
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Journal of Biological Chemistry, 1991 The present work describes the detection, purification, and characterization of a serine endopeptidase with preference for a phosphoserine in the P1' position of the substrate. During probing for the enzyme in crude extracts, as well as during its 64,000-fold purification, 32P-labeled guanidovaleryl-Arg-Ala-Ser(P)-isobutyl amide (I) was used to measure
Jonathan Rosen +3 more
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