バイBabylonia japonica REEVEの炭水化物分解酵素およびタンパク質分解酵素の性状II

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The nature of α-amylase of the mid-gut gland was further studied. The activity of cellulase and α-glucosidase was found and of saccharase could not be demonstrated in the mid-gut gland. Two proteinases were detected both in salivary gland and mid-gut gland. (1) The reaction of α-amylase in the mid-gut gland was accelerated by the addition of sodium chloride, while retarded by copper sulfate. The ions of Fe^<++>, Co^<++>, and Zn^<++> enhanced the activity of α-amylase in concentration of 10^<-3> M. (2) The optimum pH of the cellulase in the mid-gut gland was about 5.5. (3) The activity of α-glucosidase of the mid-gut gland was active at pH between 4 and 6 and catalysed the tranfer reaction of glucose residue, as evidenced by the papar chromatographic study. (4) Two proteinases contained in salivary and mid-gut gland showed the ability to split off the lower peptides from the denatured haemoglobin substrate, one of which was active at pH 3.0 and the other at neutral pH between 6.5 and 7.5. The former proteinase of the mid-gut gland was inhibited by monoiodoacetic acid, while the latter was not.
社団法人日本動物学会の論文
1961-04-15