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来自食蟹猴腮腺分泌物的富含脯氨酸的磷酸糖蛋白的氨基酸序列。

Amino acid sequence of a proline-rich phosphoglycoprotein from parotid secretion of the subhuman primate Macaca fascicularis.

作者信息

Oppenheim F G, Offner G D, Troxler R F

出版信息

J Biol Chem. 1985 Sep 5;260(19):10671-9.

PMID:4030765
Abstract

The complete amino acid sequence of the macaque proline-rich phosphoglycoprotein (MPRP) was determined by automated Edman degradation of the protein, fragments F-1 and F-2 derived from the protein by an intrinsic salivary protease, and chymotryptic, tryptic, Staphylococcus aureus V8 protease, and endoproteinase lysine-C peptides. MPRP contains 115 amino acid residues including phosphorylated serine at residues 1, 2, 6, 12, and 15, and 6 O-glycosidic carbohydrate units at residues 69, 75, 87 (threonine) and 96, 103, and 106 (serine). The Mr of the polypeptide moiety of the protein is 12,656. The amino-terminal domain contains all 5 phosphoserine residues and most of the other negatively charged and hydrophilic residues, whereas the carboxyl-terminal domain contains 24 of 25 proline residues, and 6 O-glycosidic oligosaccharides. Comparison of MPRP with the four major anionic proline-rich proteins (PRPs) from human glandular secretion shows that 57% of the amino acid residues are identical if gaps are introduced to maximize homology, suggesting that these proteins are phylogenetically related. Significant structural and functional differences occur between the macaque and human proteins. MPRP has 5 phosphoserines, PRPs have 2. MPRP is a glycoprotein, PRPs are not. MPRP inhibits the spontaneous precipitation (primary precipitation) of calcium phosphate salts from supersaturated solutions in addition to inhibiting seeded crystal growth (secondary precipitation) (Oppenheim, F. G., Offner, G. D., and Troxler, R. F. (1982) J. Biol. Chem. 257, 9271-9282), whereas PRPs inhibit only secondary precipitation. MPRP is the only major anionic proline-rich protein in macaque glandular secretion; in contrast, there are four major anionic PRPs and these display a genetic polymorphism. The significance of these structural differences with respect to biological function and the possible relationship of MPRP to salivary mucins are discussed.

摘要

通过对猕猴富含脯氨酸的磷酸糖蛋白(MPRP)进行自动Edman降解,以及对该蛋白经一种内源性唾液蛋白酶产生的F-1和F-2片段、胰凝乳蛋白酶、胰蛋白酶、金黄色葡萄球菌V8蛋白酶和赖氨酸-C内肽酶产生的肽段进行分析,确定了其完整的氨基酸序列。MPRP含有115个氨基酸残基,包括第1、2、6、12和15位残基上的磷酸化丝氨酸,以及第69、75、87(苏氨酸)和96、103、106(丝氨酸)位残基上的6个O-糖苷碳水化合物单元。该蛋白多肽部分的Mr为12,656。氨基末端结构域包含所有5个磷酸丝氨酸残基以及大多数其他带负电荷的亲水性残基,而羧基末端结构域包含25个脯氨酸残基中的24个以及6个O-糖苷寡糖。将MPRP与来自人类腺分泌液的四种主要阴离子富含脯氨酸蛋白(PRP)进行比较表明,如果引入空位以最大化同源性,57%的氨基酸残基是相同的,这表明这些蛋白在系统发育上相关。猕猴和人类蛋白之间存在显著的结构和功能差异。MPRP有5个磷酸丝氨酸,PRP有2个。MPRP是一种糖蛋白,PRP不是。除了抑制晶种晶体生长(二次沉淀)外,MPRP还抑制磷酸钙盐从过饱和溶液中的自发沉淀(一次沉淀)(奥本海姆,F.G.,奥夫纳,G.D.,和特罗克斯勒,R.F.(1982)《生物化学杂志》257,9271 - 9282),而PRP仅抑制二次沉淀。MPRP是猕猴腺分泌液中唯一主要的阴离子富含脯氨酸蛋白;相比之下,人类有四种主要的阴离子PRP,并且这些蛋白表现出遗传多态性。讨论了这些结构差异对于生物学功能的意义以及MPRP与唾液粘蛋白可能的关系。

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