| Abstrakt: |
The enzymological, physical, and immunological properties of soluble and bound forms of intracellular acid carboxypeptidase isolated from fresh mycelia of Aspergillus saitoi are reported. In the broken mycelia, about 60% of the total activity was found in the 2,000× g precipitate, with most of the remainder in the 100,000× g supernantant. The highly purified enzymes, I and I, from the 100,000× g supernatant were found to be homogeneous by such criteria as disc gel electrophoresis at pH 9.4 The bound enzyme, II, was solubilized from the 2,000× g precipitate by self-digestion at pH 6.4 and was highly purified by chromotography. The two forms of intracellular enzymes, the soluble enzymes (I and I) from the 100,00× g supernatant and the solubilized enzyme (II) from the 2,000× g precipitate, were closely related to, but not completely identical with, the extracellular acid carboxypeptidase. [ABSTRACT FROM AUTHOR] |
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