Zhidkova N I, Brewton R G, Mayne R
Department of Cell Biology, University of Alabama, Birmingham 35294.
FEBS Lett. 1993 Jul 12;326(1-3):25-8. doi: 10.1016/0014-5793(93)81753-m.
We report the molecular cloning of a proline/arginine-rich protein (called PARP) from human cartilage using the polymerase chain reaction (PCR) and degenerate oligonucleotides based on the previously published amino acid sequence of bovine PARP [1]. Subsequently, a reverse transcription-polymerase chain reaction (RT-PCR) was performed with poly(A)-rich RNA from human cartilage using a sense oligonucleotide derived from PARP and an anti-sense oligonucleotide derived from the known sequence of the human collagen alpha 2(XI) chain [2]. Nucleotide sequencing of the PCR product demonstrated that PARP is a fragment of the NH2-terminal non-collagenous (NC3) domain of the collagen alpha 2(XI) chain.
我们利用聚合酶链反应（PCR）和基于先前发表的牛脯氨酸/精氨酸丰富蛋白（PARP）氨基酸序列的简并寡核苷酸，报道了从人软骨中克隆该蛋白。随后，使用从PARP衍生的正义寡核苷酸和从人胶原蛋白α2（XI）链已知序列衍生的反义寡核苷酸，对来自人软骨的富含聚腺苷酸（poly(A)）的RNA进行逆转录-聚合酶链反应（RT-PCR）。PCR产物的核苷酸测序表明，PARP是胶原蛋白α2（XI）链NH2末端非胶原（NC3）结构域的一个片段。
