Stone S R, Hofsteenge J, Hemmings B A
Friedrich Miescher-Institut, Basel, Switzerland.
Biochemistry. 1987 Nov 17;26(23):7215-20. doi: 10.1021/bi00397a003.
Clones coding for the catalytic subunit of one of the major protein phosphatases (type 2A) were isolated from a porcine cDNA library. Sequence analysis indicated that two different mRNA species coded for this enzyme. The deduced amino acid sequences of the two forms (alpha and beta) of the enzyme were 98% identical and showed 95% identity with the partial sequence of the rabbit enzyme determined by amino acid sequencing. The use of specific oligonucleotide probes indicated that the mRNAs coding for the alpha and beta forms were about 2 kilobases in length, present in equal amounts in a porcine cell line (LLC-PK1), and were the products of two distinct genes. Southern analysis using the coding region of the alpha phosphatase cDNA as a probe suggested the existence of additional related phosphatase genes.
从猪的cDNA文库中分离出编码一种主要蛋白磷酸酶(2A型)催化亚基的克隆。序列分析表明,有两种不同的mRNA编码这种酶。该酶两种形式(α和β)推导的氨基酸序列有98%的同一性,并且与通过氨基酸测序确定的兔酶部分序列有95%的同一性。使用特异性寡核苷酸探针表明,编码α和β形式的mRNA长度约为2千碱基,在猪细胞系(LLC-PK1)中含量相等,并且是两个不同基因的产物。用α磷酸酶cDNA编码区作为探针进行的Southern分析表明存在其他相关的磷酸酶基因。