Abstract
During studies on the microbial production of acid or alkaline proteinases and an investigation of the similarities of these proteinases from the view point of enzyme-inhibitor relationships, we were successful in isolating pepsin and alkaline proteinase inhibitors. The pepsin inhibitor we isolated was found to be an acylpentapeptide which was named SPI (pepsin-inhibitor produced by Streptomyces)(1). Alkaline proteinase inhibitor, on the other hand, was found to be a protein and was abbreviated as SSI (subtilisin BPN′-inhibitor produced by Streptomyces)(2). We tried to immobilize these inhibitors and to purify the proteinases by affinity chromatography on both immobilized inhibitors.
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© 1978 Springer Science+Business Media New York
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Mitsugi, K., Miyajima, R., Satoi, H., Sato, S., Murao, S. (1978). Purification of Proteinases by Affinity Chromatography Techniques. In: Pye, E.K., Weetall, H.H. (eds) Enzyme Engineering. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-5163-5_37
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DOI: https://doi.org/10.1007/978-1-4757-5163-5_37
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