Himeno M, Noguchi Y, Sasaki H, Tanaka Y, Furuno K, Kono A, Sakaki Y, Kato K
Division of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Kyushu University, Fukuoka, Japan.
FEBS Lett. 1989 Feb 27;244(2):351-6. doi: 10.1016/0014-5793(89)80561-7.
A cDNA for 107 kDa sialoglycoprotein (LGP 107), the major protein component of rat liver lysosomal membranes, was isolated and sequenced. The 1.8 kbp cDNA contained an open reading frame encoding a polypeptide consisting of 386 amino acid residues (Mr 41,914). The deduced NH2-terminal 10-residue sequence is identical with that determined for purified LGP 107. The primary structure deduced for LGP 107 contains 20 potential N-glycosylation sites and exhibits 82.5, 43 and 60% sequence similarities to mouse LAMP-1, chicken LEP 100, and a 120-kDa human lysosomal glycoprotein, respectively. Among these lysosomal glycoproteins, the amino acid sequence of the putative transmembrane segment is highly conserved. Northern blot hybridization analysis identified a single species of LGP 107 mRNA (2.1 kbp in length) in rat liver, kidney, brain, lung, spleen, heart and pancreas, although its level in pancreas was very low.
分离并测序了大鼠肝脏溶酶体膜主要蛋白质成分107kDa唾液酸糖蛋白（LGP 107）的cDNA。该1.8kbp的cDNA包含一个开放阅读框，编码一个由386个氨基酸残基组成的多肽（Mr 41,914）。推导的NH2末端10个残基的序列与纯化的LGP 107测定的序列相同。推导的LGP 107一级结构包含20个潜在的N-糖基化位点，与小鼠LAMP-1、鸡LEP 100和一种120kDa的人溶酶体糖蛋白的序列相似性分别为82.5%、43%和60%。在这些溶酶体糖蛋白中，假定跨膜区的氨基酸序列高度保守。Northern印迹杂交分析在大鼠肝脏、肾脏、大脑、肺、脾脏、心脏和胰腺中鉴定出单一的LGP 107 mRNA（长度为2.1kbp），尽管其在胰腺中的水平非常低。
