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Frog albumin is expressed in skin and characterized as a novel potent trypsin inhibitor
Zhang YX1,2; Lai R1; Lee WH1; Zhang Y*1; zhangy@mail.kiz.ac.cn
2005
发表期刊PROTEIN SCIENCE
ISSN0961-8368
卷号14期号:9页码:2469-2477
摘要A novel potent trypsin inhibitor was purified and characterized from frog Bombina maxima skin. A full-length cDNA encoding the protein was obtained from a cDNA library constructed from the skin. Sequence analysis established that the protein actually comprises three conserved albumin domains. B.maxima serum albumin was subsequently purified, and its coding cDNA was further obtained by PCR-based cloning from the frog liver. Only two amino acid variations were found in the albumin sequences from the skin and the serum. However, the skin protein is distinct from the serum protein by binding of a haem b (0.95 mol/mol protein). Different from bovine serum albumin, B. maxima albumin potently inhibited trypsin. It bound tightly with trypsin in a 1:1 molar ratio. The equilibrium dissociation constants (KD) obtained for the skin and the serum proteins were 1.92 x 10(-9) M and 1.55 x 10(-9) M, respectively. B. maxima albumin formed a noncovalent complex with trypsin through an exposed loop formed by a disulfide bond (Cys53-Cys62), which comprises the scissile bond Arg58(P1)-His59(P1'). No inhibitory effects on thrombin, chymotrypsin, elastase, and subtilisin were observed under the assay conditions. Immunohistochemical study showed that B. maxima albumin is widely distributed around the membranes of epithelial layer cells and within the stratum spongiosum of dermis in the skin, suggesting that it plays important roles in skin physiological functions, such as water economy, metabolite exchange, and osmoregulation.
关键词Albumin Skin Trypsin Haem Amphibian Frog
资助者This work was supported by the grants of Western Light, projects from the Chinese Academy of Sciences (Y.Z., W.H.L.), and grants from National Natural Science Founda- tion (30170195, 30470380, 30200044) and Yunnan Science and Technology Commission (2003C0066M). ; This work was supported by the grants of Western Light, projects from the Chinese Academy of Sciences (Y.Z., W.H.L.), and grants from National Natural Science Founda- tion (30170195, 30470380, 30200044) and Yunnan Science and Technology Commission (2003C0066M). ; This work was supported by the grants of Western Light, projects from the Chinese Academy of Sciences (Y.Z., W.H.L.), and grants from National Natural Science Founda- tion (30170195, 30470380, 30200044) and Yunnan Science and Technology Commission (2003C0066M). ; This work was supported by the grants of Western Light, projects from the Chinese Academy of Sciences (Y.Z., W.H.L.), and grants from National Natural Science Founda- tion (30170195, 30470380, 30200044) and Yunnan Science and Technology Commission (2003C0066M).
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资助者This work was supported by the grants of Western Light, projects from the Chinese Academy of Sciences (Y.Z., W.H.L.), and grants from National Natural Science Founda- tion (30170195, 30470380, 30200044) and Yunnan Science and Technology Commission (2003C0066M). ; This work was supported by the grants of Western Light, projects from the Chinese Academy of Sciences (Y.Z., W.H.L.), and grants from National Natural Science Founda- tion (30170195, 30470380, 30200044) and Yunnan Science and Technology Commission (2003C0066M). ; This work was supported by the grants of Western Light, projects from the Chinese Academy of Sciences (Y.Z., W.H.L.), and grants from National Natural Science Founda- tion (30170195, 30470380, 30200044) and Yunnan Science and Technology Commission (2003C0066M). ; This work was supported by the grants of Western Light, projects from the Chinese Academy of Sciences (Y.Z., W.H.L.), and grants from National Natural Science Founda- tion (30170195, 30470380, 30200044) and Yunnan Science and Technology Commission (2003C0066M).
文献类型期刊论文
条目标识符http://ir.kiz.ac.cn/handle/152453/2669
专题科研部门_生物毒素与人类疾病(张云)
科研部门_天然药物功能蛋白质学科组(赖仞)
通讯作者zhangy@mail.kiz.ac.cn
作者单位1.Department of Animal Toxinology, Kunming Institute of Zoology, The Chinese Academy of Sciences, Kunming, Yunnan 650223, China (PRC)
2.Graduate School of the Chinese Academy of Sciences, Beijing 100039, China (PRC)
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Zhang YX,Lai R,Lee WH,et al. Frog albumin is expressed in skin and characterized as a novel potent trypsin inhibitor[J]. PROTEIN SCIENCE,2005,14(9):2469-2477.
APA Zhang YX,Lai R,Lee WH,Zhang Y*,&zhangy@mail.kiz.ac.cn.(2005).Frog albumin is expressed in skin and characterized as a novel potent trypsin inhibitor.PROTEIN SCIENCE,14(9),2469-2477.
MLA Zhang YX,et al."Frog albumin is expressed in skin and characterized as a novel potent trypsin inhibitor".PROTEIN SCIENCE 14.9(2005):2469-2477.
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