Elstow S F, Weiss J B
Coll Relat Res. 1983 May;3(3):181-93. doi: 10.1016/s0174-173x(83)80002-8.
Collagen was extracted with neutral salt solution and examined for the presence of type V collagen. A fraction which was insoluble in both 0.02 M Na2HPO4, pH 9.2 and phosphate-buffered saline (PBS) pH 7.2 at 4 degrees C contained both alpha 1(V)- and alpha 2(V)-chains demonstrated by sodium dodecyl sulfate polyacrylamide gel electrophoresis, diethylaminoethyl cellulose ion exchange chromatography, amino acid analysis and segment long spacing (SLS) crystallites. SLS crystallites showed a globular N-terminal extension peptide attached to the type V collagen monomer. Ion exchange chromatography also demonstrated the presence of a third, minor component, which was identified as the alpha 3(V)-chain. In certain extractions, components corresponding to the partially processed procollagen chains of type V collagen were also observed.
用中性盐溶液提取胶原蛋白，并检测Ⅴ型胶原蛋白的存在情况。在4℃下，一种在0.02M Na2HPO4（pH 9.2）和磷酸盐缓冲盐水（PBS，pH 7.2）中均不溶的组分，经十二烷基硫酸钠聚丙烯酰胺凝胶电泳、二乙氨基乙基纤维素离子交换色谱、氨基酸分析和片段长间距（SLS）微晶分析，证实含有α1（Ⅴ）链和α2（Ⅴ）链。SLS微晶显示Ⅴ型胶原蛋白单体上连接有一个球状的N端延伸肽。离子交换色谱还证实存在第三种次要成分，鉴定为α3（Ⅴ）链。在某些提取物中，还观察到了与Ⅴ型胶原蛋白部分加工的前胶原链相对应的成分。
