The primary structure and functional characterization of the neutral histidine-rich polypeptide from human parotid secretion.

The primary structure and functional characterization of the neutral histidine-rich polypeptide from human parotid secretion.
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DOI:
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发表时间:
1986-01
期刊:
The Journal of biological chemistry
影响因子:
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通讯作者:
F. Oppenheim;Y. Yang;R. Diamond;D. Hyslop;G. Offner;R. Troxler
F. Oppenheim;Y. Yang;R. Diamond;D. Hyslop;G. Offner;R. Troxler
中科院分区:
其他
文献类型:
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作者:
F. Oppenheim;Y. Yang;R. Diamond;D. Hyslop;G. Offner;R. Troxler

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用离子交换层析和凝胶过滤层析从人腮腺分泌物中分离出中性富组氨酸多肽(HRP)。通过自动Edman降解蛋白质、胰蛋白酶和金黄色葡萄球菌V8蛋白酶肽,并用羧肽酶A消化测定的完整氨基酸序列为:(式:见正文)其中Pse代表磷酸丝氨酸。该多肽含有38个残基,Mr为4929。带电荷的氨基酸以7个组氨酸、4个精氨酸、3个赖氨酸、3个天冬氨酸、3个谷氨酸残基和1个磷酸丝氨酸为主。假设在pH 7时组氨酸的电荷贡献最小,磷酸丝氨酸的负电荷最小,则HRP的净电荷由碱性和酸性残基的相等贡献平衡。此外,亲水性和疏水性残基沿着多肽链的分布表明不存在结构极性。该多肽缺乏苏氨酸、丙氨酸、缬氨酸、半胱氨酸、甲硫氨酸和异亮氨酸。HRP与美国国家生物医学研究基金会数据库中的任何蛋白质序列都没有显示出序列相似性。HRP是从相对于磷酸钙盐过饱和的溶液中羟基磷灰石晶体生长的活性抑制剂,因此必须在口腔流体中的矿物-溶质相互作用的稳定中发挥作用。此外,HRP是一种有效的白色念珠菌发芽抑制剂,因此可能是口腔中抗微生物宿主防御系统的重要组成部分。
The neutral histidine-rich polypeptide (HRP) from human parotid secretion was isolated by ion-exchange and gel-filtration chromatography. The complete amino acid sequence determined by automated Edman degradation of the protein, tryptic and Staphylococcus aureus V8 protease peptides, and digestion with carboxypeptidase A is: (Formula: see text) where Pse represents phosphoserine. The polypeptide contains 38 residues and has Mr 4929. The charged amino acids predominate with 7 histidine, 4 arginine, 3 lysine, 3 aspartic acid, 3 glutamic acid residues, and 1 phosphoserine. Assuming minimal charge contributions from histidine and one negative charge from phosphoserine at pH 7, the net charge of HRP is balanced by an equal contribution of basic and acidic residues. Furthermore, the distribution of hydrophilic and hydrophobic residues along the polypeptide chain indicates that there is no structural polarity. The polypeptide lacks threonine, alanine, valine, cysteine, methionine, and isoleucine. HRP did not display sequence similarity with any protein sequence in the National Biomedical Research Foundation Data Bank. HRP is an active inhibitor of hydroxyapatite crystal growth from solutions supersaturated with respect to calcium phosphate salts and therefore must play a role in the stabilization of mineral-solute interactions in oral fluid. In addition, HRP is a potent inhibitor of Candida albicans germination and therefore may be a significant component of the antimicrobial host defense system in the oral cavity.