Cooperativity between pepsin and crystallization of calcium carbonate in distilled water

被引:19
作者
Yang, L [1 ]
Guo, YM [1 ]
Ma, XM [1 ]
Hu, ZG [1 ]
Zhu, SF [1 ]
Zhang, XY [1 ]
Jiang, K [1 ]
机构
[1] Henan Normal Univ, Coll Chem & Environm Sci, Xinxiang 453002, Peoples R China
基金
中国国家自然科学基金;
关键词
cooperativity; calcium carbonate; pepsin; secondary structure;
D O I
10.1016/S0162-0134(02)00573-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Cooperativity between pepsin and crystallization of calcium carbonate in distilled water was studied. The results show that vaterite was formed under the influence of pepsin and the crystalline product was a composite of vaterite and pepsin. The component of this material was similar to that of nacre. At the same time, the crystallization of calcium carbonate had also an important effect on the secondary structure of the pepsin. The secondary structure of the pepsin was characterized through FT-IR technology. The result indicated that the pure pepsin is composed of 24.38% alpha-helices, 29.91% beta-sheets, 39.32% beta-turns and 6.49% random structures and the pepsin in the CaCO3-pepsin solution is composed of 2.09% alpha-helices, 93.304% beta-sheets, 4.592% beta-turns and 0.006% random structure. During the crystallization of the calcium carbonate from the pepsin solution, the secondary structure of the pepsin transformed. These results showed that there was cooperativity between the crystallization of vaterite and the pepsin. The cooperative mechanism is discussed. (C) 2002 Elsevier Science Inc. All rights reserved.
引用
收藏
页码:197 / 203
页数:7
相关论文
共 29 条
[1]   Control of crystal phase switching and orientation by soluble mollusc-shell proteins [J].
Belcher, AM ;
Wu, XH ;
Christensen, RJ ;
Hansma, PK ;
Stucky, GD ;
Morse, DE .
NATURE, 1996, 381 (6577) :56-58
[2]   BIOLOGICAL-CONTROL OF CRYSTAL TEXTURE - A WIDESPREAD STRATEGY FOR ADAPTING CRYSTAL PROPERTIES TO FUNCTION [J].
BERMAN, A ;
HANSON, J ;
LEISEROWITZ, L ;
KOETZLE, TF ;
WEINER, S ;
ADDADI, L .
SCIENCE, 1993, 259 (5096) :776-779
[3]   EXAMINATION OF THE SECONDARY STRUCTURE OF PROTEINS BY DECONVOLVED FTIR SPECTRA [J].
BYLER, DM ;
SUSI, H .
BIOPOLYMERS, 1986, 25 (03) :469-487
[4]   BIOSYNTHESIS OF CADMIUM-SULFIDE QUANTUM SEMICONDUCTOR CRYSTALLITES [J].
DAMERON, CT ;
REESE, RN ;
MEHRA, RK ;
KORTAN, AR ;
CARROLL, PJ ;
STEIGERWALD, ML ;
BRUS, LE ;
WINGE, DR .
NATURE, 1989, 338 (6216) :596-597
[5]   Control of aragonite or calcite polymorphism by mollusk shell macromolecules [J].
Falini, G ;
Albeck, S ;
Weiner, S ;
Addadi, L .
SCIENCE, 1996, 271 (5245) :67-69
[6]   Simulation of biomimetic recognition between polymers and surfaces [J].
Golumbfskie, AJ ;
Pande, VS ;
Chakraborty, AK .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (21) :11707-11712
[7]   SECONDARY STRUCTURE OF THE MEMBRANE-BOUND FORM OF THE PORE-FORMING DOMAIN OF COLICIN-A - AN ATTENUATED TOTAL-REFLECTION POLARIZED FOURIER-TRANSFORM INFRARED-SPECTROSCOPY STUDY [J].
GOORMAGHTIGH, E ;
VIGNERON, L ;
KNIBIEHLER, M ;
LAZDUNSKI, C ;
RUYSSCHAERT, JM .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1991, 202 (03) :1299-1305
[8]  
HARRISON PM, 1989, BIOMINERALISATION, P295
[9]   Molecular mechanism of the nacreous layer formation in Pinctada maxima [J].
Kono, M ;
Hayashi, N ;
Samata, T .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2000, 269 (01) :213-218
[10]  
Lowenstam H. A., 1989, BIOMINERALIZATION