1972
DOI: 10.1093/oxfordjournals.jbchem.a129739
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Inactivation of Acid Proteases from Rhizopus chinensis, Aspergillus saitoi and Mucor pusillus, and Calf Rennin by Diazoacetylnorleucine Methyl Ester*

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Cited by 62 publications
(8 citation statements)
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“…145 Using these techniques, novel acid proteases were classified based on their propensity to be inactivated by a diazo compound. 146152 Nonetheless, with the advent of site-directed mutagenesis, the use of diazo compounds to characterize proteins became rare.…”
Section: Protein Alkylationmentioning
confidence: 99%
“…145 Using these techniques, novel acid proteases were classified based on their propensity to be inactivated by a diazo compound. 146152 Nonetheless, with the advent of site-directed mutagenesis, the use of diazo compounds to characterize proteins became rare.…”
Section: Protein Alkylationmentioning
confidence: 99%
“…The enzyme has been partially purified from A. turbidans ATCC 9325 and displayed a strong ester hydrolase activity with IX-amino acid esters only. The Km for cephalexin deacylation was 2.99 mM (Takahashi et al 1972;. The enzyme also displayed IX-amino-acyltransferase activity in the presence of suitable acyl receptors such as 7-ADCA to produce cephalexin .…”
Section: C) Bioconversion Of Cephalosporins and Of 6-apa With \I-aminmentioning
confidence: 96%
“…R. chinensis was cultured for 70 hrs at 25°C on wheat bran for protease production (Fukumoto et aL 1967). (Graham et al 1973;Mizobe et al 1973;Nakamura 1977Nakamura , 1978Sepulveda et al 1975;Subramanian 1978;Subramanian et al 1977;Takahashi et aL 1972;Tsuru et al 1969). It belongs to the pepsin type, has a pH optimum between 2.9 and 3.2 and its temperature optimum at 60°C.…”
Section: Fermentationmentioning
confidence: 99%
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“…(α) 'Εστεροποίηση_των_καρ3οξυλομάδων_τής_καθ Ή έστεροποίηση τών καρβοξυλομάδων πολλών όξινων πρωτεασών κατορθώ θηκε μέ τήν χρησιμοποίηση διαζωενώσεων. Τά ένζυμα αυτά είναι: ή όξινη πρωτεάση τοΰ θυρεοειδούς (Smith et al, 1969), οί όξινες πρωτεάσες τών μυκήτων Rhizopus Chinensis, Aspergillus Niger καί Mucor Pusillus (Takahashi et al, 1972) καί οί καθεψίνες D καί E (Keilova, 1970' Keilova & Lapresle, 1970' Ferguson et al, 1973' Rakitzis, 1974. Σέ δλες τίς περιπτώσεις πού κατορθώθηκε ή έστεροποίηση τών καρβοξυλίων της καθε ψίνης D, ή άλλων όξινων πρωτεασών, παρατηρήθηκε καί απώλεια τής ένζυμικής δραστικότητας.…”
Section: προηγούμεγες_προσπάθειες_χημίκης_ΐροποποίησης_της_καθεφίγης_[χunclassified