Properties of a New Alkaline Proteinase from Aspergillus niger
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概要
- 論文の詳細を見る
A. niger LCF 9 synthesizes a new aspergillopeptidase of potential interest in therapeutics. The properties and operating range of the enzyme were determined. It is a semi-alkaline aspergillopeptidase (EC 3.4.23.4) with one endopeptidase activity. Its pI is 4.10,its molecular weight is 21000 Da and its A^<1%>_<1cm> at 280 nm is 9.75. It rapidly hydrolyzes casein and hemoglobin. Its optimal pH is 7.8 and optimal temperature is 45℃. It is thermally labile above 40℃ but can be stabilized by adding calcium ions. It is inhibited by phenylmethylsulfonyl fluoride (PMSF), by ethylenediaminetetraacetic acid (EDTA) and by certain metals ions, e.g. copper, manganese and cobalt ions. It has no dipeptidase or tripeptidase activity and its esterase activity is weak. It has a high collagenase activity and is to our knowledge the only aspergillopeptidase that is active toward benzoyl-arginine p-nitroanilide (BAPNA).
- 公益社団法人日本薬学会の論文
- 1989-05-25
著者
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POURRAT Aimee
Laboratoire de Pharmacie Galenique et Pharmacotechnie Industrielle
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POURRAT HENRI
Laboratoire de Pharmacie Galenique et Pharmacotechnie
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Pourrat A
Laboratoire De Pharmacie Galenique Et Pharmacotechnie Industrielle
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Pourrat H
Laboratoire De Pharmacognosie Et Biotechnologie
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BARTHOMEUF Chantal
Laboratoire de Pharmacognosie et Biotechnologie
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Barthomeuf C
Laboratoire De Pharmacognosie Et Biotechnologie
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