The proteolytic enzymes of microorganisms: VII. A study of some of the properties of two proteases isolated from Mortierella renispora dixon-stewart

DOI	Trouver le DOI : https://doi.org/10.1139/y54-008
Auteur	Rechercher : Wetter, L. R.¹
Affiliation	Conseil national de recherches du Canada. Laboratoire régional des prairies
Format	Texte, Article
Résumé	Two proteases isolated from the culture medium of Mortierella renispora Dixon-Stewart (PRL 26) had different isoelectric points but similar pH optimums. The components were inhibited by equal amounts of ovomucoid. Heat studies showed that the constituent moving towards the cathode (cathodic component) was more stable at 58 °C. than the anodic component. The enzyme located in the cathodic component hydrolzyed chloroacetyl-L-tyrosine. The same fraction also hydrolyzed N-carbobenzoxy-α-L-glutamyl-DL-alanine and to a much lesser extent N-carbobenzoxy-α-L-glutamyl-L-glutamic acid. No enzymatic activity could be detected against glycylglycine, diglycylglycine, glycyl-L-proline, seryl-serine, or α-benzoyl-L-argininamide.
Date de publication	1954-01-01
Maison d’édition	Canadian Science Publisher
Dans	Canadian Journal of Biochemistry and Physiology 32, nº 1 (1 janvier 1954) : 60–67.
Langue	anglais
Publications évaluées par des pairs	Oui
Identificateur	NRCC-3131
Exporter la notice	Exporter en format RIS
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Enregistrement modifié	2023-09-05