Abstract
Taka-amylase A was resistant to the action of proteolytic enzymes, but when one mole of phenylazobenzoyl group was introduced into the enzyme derivative, phenylazo-benzoyl-taka-amylase A became susceptible to the various proteases. It was, therefore, suggested that the introduction of phenylazo-benzoyl group might alter molecular conformation of intact TAA, as also supported by the changes in specific optical rotation and reduced viscosity.
Partial degradation of PhAB-TAA by “pronase” was investigated. Proteolytically modified PhAB-TAA (M-PhAB-TAA) was iso-lated in a crystalline form and its chromatographic behavior and homogeneity were investigated with the aid of DEAE-cellulose.
The authors are grateful to Prof. K. Narita and Dr. T. Ikenaka for their kind guidances and valuable discussions through this investigation, to Dr. M. Nomoto for his generous gift of “pronase” and also to Sankyo Co., Ltd. for their kind supply of “Takadiastase Sankyo”.
