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  • Title: [Carboxylic proteinases from the microscopic fungi Trichoderma viride and Trichoderma lignorum].
    Author: Gaĭda AV, Osterman AL, Rudenskaia GN, Stepanov VM.
    Journal: Biokhimiia; 1981 Jan; 46(1):181-9. PubMed ID: 7018591.
    Abstract:
    Using ion-exchange chromatography on aminosilochrome and biospecific chromatography on Bacitracin-Sepharose, the carboxylic proteinases have been isolated for the first time from the microscopic fungi of the Trichoderma genus -- Trichoderma viride and Trichoderma lignorum, commonly used to produce cellulases. The proteinases are stable within the pH range of 3 to 6; pI is 4,3 and 4,5, the pH optimum -- 2,3 and 2,8, respectively. The molecular weight of the enzymes is 32000, the amino acid composition of T. viride proteinase is Lys5His2Arg6Asx27Thr39Ser38Glx27Pro13..Gly41Ala28Cys2Val37Ile11Leu17Tyr13Phe11Trp3, that of T. lignorum is Lys9His4Arg6Asx36Thr26Ser46Glx25Pro14Gly35Ala23Cys2Val28Ile26Leu19Tyr12..Phe14Trp4. Both enzymes are completely inactivated by specific inhibitors of carboxylic proteinase, i. e. pepstatin, diazoacetyl-D,L-norvaline methylester and N-diazoacetyl-N'-2,4-dinitrophenylethylenediamine. The molecular and enzymatic properties of the proteinases under study are close to those of carboxylic proteinases of microscopic fungi and in a lesser degree to those of porcine pepsin.
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