Abstract
The enzymological, physical, and immunological properties of soluble and bound forms of intracellular acid carboxypeptidase isolated from fresh mycelia ofAspergillus 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, Ia and Ib, 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 (Ia and Ib) 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.
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Ichishima, E., Tsuruda, Y., Ushijima, T. et al. Soluble and bound forms of intracellular acid carboxypeptidase inAspergillus saitoi . Current Microbiology 4, 85–89 (1980). https://doi.org/10.1007/BF02602898
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DOI: https://doi.org/10.1007/BF02602898