Statements in which the resource exists.
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pubmed-article:15638pubmed:abstractTextMetal and serine proteases were separated on the biospecific sorbent. Two different, homogeneous metal proteases were obtained by rechromatography of the metal protease. Activation energies, heat stability, molecular weights, influence of inhibitors, the dependence of activity on pH and temperature were determined. Properties of two metal proteases were compared with those of literary analogs.lld:pubmed
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pubmed-article:15638pubmed:monthOctlld:pubmed
pubmed-article:15638pubmed:issn0320-9725lld:pubmed
pubmed-article:15638pubmed:authorpubmed-author:GlemzhaA AAAlld:pubmed
pubmed-article:15638pubmed:authorpubmed-author:PalubinskasV...lld:pubmed
pubmed-article:15638pubmed:authorpubmed-author:VesaV SVSlld:pubmed
pubmed-article:15638pubmed:authorpubmed-author:BeliauskaiteI...lld:pubmed
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pubmed-article:15638pubmed:volume41lld:pubmed
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pubmed-article:15638pubmed:pagination1798-1802lld:pubmed
pubmed-article:15638pubmed:dateRevised2007-7-23lld:pubmed
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pubmed-article:15638pubmed:year1976lld:pubmed
pubmed-article:15638pubmed:articleTitle[Metal proteases from Bac. subtilis].lld:pubmed
pubmed-article:15638pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15638pubmed:publicationTypeEnglish Abstractlld:pubmed