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- W1571836700 abstract "Alkali-dissociated Fraction II prepared by an improved technique from bovine procarboxypeptidase A-S6 (procarboxypeptidase A with a sedimentation coefficient of 6 S) was found to be heterogeneous and was resolved into three subfractions; IIa, IIb and IIc by equilibrium chromatography on CM-Sephadex at pH 6.0. Subfractions IIb and IIc could be activated by trypsin to give an N-acetyl-l-tyrosine ethyl ester (ATEE)-splitting endopeptidase whereas IIa was not activated. Subfraction IIb was shown to be an artifact slowly arising from IIc under the conditions prevailing during the dissociation step. The two Subfractions IIb and IIc were observed to have practically the same amino acid composition, sedimentation constant (2.9 S), molecular weight (28 500) and terminal residues (N-terminal half-cystine and C-terminal leucine). All these values demonstrate the very high degree of homology existing between subunit II and porcine chymotrypsinogen C. Subfractions IIb and IIc were activated at a much slower rate than undissociated subunit II and the kcat of the corresponding ATEE-splitting reaction was also somewhat reduced. However, like activated subunit II, the activated subfractions were found to possess not less than 0.8 active site per mole. The somewhat lower molecular weight of Subfraction IIa (27 000) and the presence of one N-terminal aspartic acid (or asparagine) pointed out the possibility that this subfraction was a slightly modified form of Fraction III." @default.
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- W1571836700 date "1972-08-01" @default.
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- W1571836700 title "On subunit II of bovine procarboxypeptidase A" @default.
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- W1571836700 doi "https://doi.org/10.1016/0005-2744(72)91012-1" @default.
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