Towatari T, Katunuma N
Division of Enzyme Chemistry, University of Tokushima, Japan.
FEBS Lett. 1988 Aug 15;236(1):57-61. doi: 10.1016/0014-5793(88)80285-0.
The complete amino acid sequences of the heavy and light chains of rat liver cathepsin L (EC 3.4.22.15) were determined at the protein level. The heavy and light chains consisted of 175 and 44 amino acid residues, respectively, and their Mr values without glycosyl groups calculated from these sequences were 18941 and 5056, respectively. The amino acid sequence was also determined from the N-terminal sequences of the heavy and light chains, and the sequences of cleavage fragments of the heavy chain with lysylendopeptidase and cyanogen bromide. The fragments were aligned by comparison with the amino acid sequence deduced from the sequence of cDNA of rat preprocathepsin L. The sequence of rat liver cathepsin L determined at the protein level was identical with that deduced from the cDNA sequence except that in the heavy chain, residues 176-177 (Asp-Ser) were not present at the C-terminus and alanine was replaced by proline at residue 125. Asn-108 in the heavy chain is modified with carbohydrate.
测定了大鼠肝脏组织蛋白酶L(EC 3.4.22.15)重链和轻链完整的氨基酸序列。重链和轻链分别由175和44个氨基酸残基组成,根据这些序列计算,其无糖基化修饰时的Mr值分别为18941和5056。还通过重链和轻链的N端序列以及重链用赖氨酰内肽酶和溴化氰切割片段的序列来确定氨基酸序列。通过与从大鼠组织蛋白酶L前体cDNA序列推导的氨基酸序列进行比较来比对这些片段。在蛋白质水平测定的大鼠肝脏组织蛋白酶L的序列与从cDNA序列推导的序列相同,只是在重链中,C端不存在176 - 177位残基(天冬氨酸 - 丝氨酸),并且在125位残基处丙氨酸被脯氨酸取代。重链中的天冬酰胺 - 108被碳水化合物修饰。