Primary structure of the telopeptide and a portion of the helical domain of chicken type II procollagen as determined by DNA sequence analysis.
Primary structure of the telopeptide and a portion of the helical domain of chicken type II procollagen as determined by DNA sequence analysis.
复制标题
DOI：
10.1042/bj2290189
复制
发表时间：
1985-07
期刊：
影响因子：
--
通讯作者：
F. Deák;W. Argraves;I. Kiss;K. Sparks;P. Goetinck
中科院分区：
文献类型：
--
作者：
F. Deák;W. Argraves;I. Kiss;K. Sparks;P. Goetinck
鸡II型前胶原的三个新的cDNA克隆的核苷酸序列与其他三种类型的鸡原纤维前胶原的序列的比较表明，最保守的区域与羟脯氨酸，羟赖氨酸，半胱氨酸和赖氨酸残基的位置相关。通过对α 1（II）和α 1（I）前胶原的分离位点的计算，发现α 1（II）和α 1（I）前胶原的分离晚于α 1（I）和α 2（I）前胶原。
A comparison of the nucleotide sequences of three new cDNA clones for chicken type II procollagen with the sequences of the other three types of chicken fibrillar procollagens reveals that the most conserved regions correlate with the positions of hydroxyproline, hydroxylysine, cysteine and lysine residues. On the basis of replacement-site-divergence calculations it is concluded that alpha 1(II) and alpha 1(I) procollagens diverged later than alpha 1(I) and alpha 2(I) procollagens.