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FEBS Lett. 1993 Mar 29;320(1):35-7.

Amino acid sequence of alkaliphilic serine protease from silkworm, Bombyx mori, larval digestive juice.

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  • 1Department of Food Science and Technology, School of Agriculture, Nagoya University, Aichi, Japan.


Alkaliphilic protease, P-IIc, from silkworm, Bombyx mori, larval midgut digestive juice consists of 232 amino acids. It has a catalytic triad, Asp-His-Ser, invariably found in a serine protease. A shift of optimal pH value towards the alkaline side diminished at mu = 1.0. This suggests the existence of an electrostatic interaction that affects the proteolytic activity. The higher Arg content may be responsible for this phenomenon. Two cysteine residues probably exist unpaired in a novel position among serine proteases.

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