N40, a Novel Nonacidic Matrix Protein from Pearl Oyster Nacre, Facilitates Nucleation of Aragonite in Vitro

A novel nonacidic matrix protein from pearl oyster nacre has been purified by cation-exchange chromatography. It was designated N40 for the nacreous protein of approximately 40 kDa. On the basis of the extraction method (with Tris-buffered Milli-Q water) and amino acid compositions (Gly- and Ala-ric...

Full description

Saved in:
Bibliographic Details
Published in:Biomacromolecules 2007-11, Vol.8 (11), p.3597-3601
Main Authors: Yan, Zhenguang, Jing, Gu, Gong, Ningping, Li, Changzhong, Zhou, Yujuan, Xie, Liping, Zhang, Rongqing
Format: Article
Language:English
Subjects:
Acids - chemistry
Amino Acids - metabolism
Analytical, structural and metabolic biochemistry
Animals
Applied sciences
Biological and medical sciences
Calcium Carbonate - chemistry
Exact sciences and technology
Fundamental and applied biological sciences. Psychology
Hydrogen-Ion Concentration
Microscopy, Electron, Scanning
Miscellaneous
Natural polymers
Physicochemistry of polymers
Pinctada - chemistry
Pinctada - metabolism
Proteins
Proteins - chemistry
Proteins - isolation & purification
Proteins - metabolism
Proteins - ultrastructure
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Spectroscopy, Fourier Transform Infrared
Spectrum Analysis, Raman
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:A novel nonacidic matrix protein from pearl oyster nacre has been purified by cation-exchange chromatography. It was designated N40 for the nacreous protein of approximately 40 kDa. On the basis of the extraction method (with Tris-buffered Milli-Q water) and amino acid compositions (Gly- and Ala-rich), N40 was inferred to be a conventional “insoluble matrix protein”. Crystallization experiments showed that N40 could facilitate the nucleation of aragonite drastically. So far, among the macromolecules that have been purified from the shell, N40 is an exclusive protein that can nucleate aragonite by itself, without the need for adsorption to a substrate. Thus, the present study has proposed the possibility that the nonacidic shell protein (maybe a conventional “insoluble framework protein”) can also directly participate in aragonite nucleation and even act as a nucleation site. It is a valuable supplement to the classic biomineralization theory, in which the soluble acidic proteins of the shell are generally believed to function as a nucleation site.
ISSN:1525-7797
1526-4602
DOI:10.1021/bm0701494