The use of diethylpyrocarbonate to inhibit endogenous ribonuclease in sheep pancreas allows the detection of protein-disulphide-isomerase activity in homogenates, at specific activities of up to 4 units/g. This is higher than the specific activity in sheep liver homogenates (about 2 units/g) or in homogenates of other sheep tissues (16). It is thus evident that high levels of protein-disulphide-isomerase activity are present in sheep pancreas. This is consistent both with the postulated general role of protein disulphide-isomerase in protein biosynthesis (10,11) and with the in vitro action of the enzyme on its conventional substrate scrambled ribonuclease, since pancreas is the major site of ribonuclease synthesis.
Research Article| May 01 1982
Detection of protein disulphide-isomerase in sheep pancreas fractions
David A. Hillson;
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David A. Hillson, Jacqueline Anderson; Detection of protein disulphide-isomerase in sheep pancreas fractions. Biosci Rep 1 May 1982; 2 (5): 343–349. doi: https://doi.org/10.1007/BF01115120
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