大鼠唾液腺肽基甘氨酸α-酰胺化单加氧酶（PAM）的分泌

Secretion of peptidylglycine alpha-amidating monooxygenase (PAM) from rat salivary glands.

作者信息

Kato T, Hanaoka K, Ochiai O, Chikuma T, Takeda K, Yajima R, Kumegawa M

机构信息

Laboratory of Molecular Recognition, Graduate School of Integrated Science, Yokohama City University, Japan.

出版信息

Neurochem Int. 1992 Sep;21(2):153-8. doi: 10.1016/0197-0186(92)90141-d.

DOI:10.1016/0197-0186(92)90141-d

PMID:1303147

Abstract

Peptidylglycine alpha-amidating monooxygenase (PAM) is a regulating enzyme to synthesize the biologically active hormones having carboxy-terminal amide. In the present study we investigated secretion of the enzyme from rat saliva. Property of PAM in the saliva was similar to that in the submandibular gland. Both enzymes showed similar pH optimum at 5.0 and optimal ascorbic acid concentration at 2.5 mM. But molecular size of PAM in the saliva was 75 kDa in the gel permeation chromatography on Superose 12 column, while the size in the submandibular gland was 25 kDa. After the treatment with trypsin, PAM in the saliva was converted to a small size molecule, which is similar to the size in rat submandibular gland. These and other data indicate that a native molecular size of PAM is secreted into saliva and plays some physiological roles.

摘要

肽基甘氨酸α-酰胺化单加氧酶（PAM）是一种调节酶，用于合成具有羧基末端酰胺的生物活性激素。在本研究中，我们研究了该酶从大鼠唾液中的分泌情况。唾液中PAM的特性与下颌下腺中的相似。两种酶在pH 5.0时显示出相似的最适pH值，在抗坏血酸浓度为2.5 mM时显示出最佳活性。但是，在Superose 12柱上进行凝胶渗透色谱分析时，唾液中PAM的分子大小为75 kDa，而下颌下腺中的大小为25 kDa。用胰蛋白酶处理后，唾液中的PAM转化为小分子，其大小与大鼠下颌下腺中的相似。这些数据和其他数据表明，PAM的天然分子大小被分泌到唾液中并发挥一些生理作用。