Amino-acid sequence of porcine pepsin.
Amino-acid sequence of porcine pepsin.
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DOI：
10.1073/pnas.70.12.3437
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发表时间：
1973-12
影响因子：
11.1
通讯作者：
J. Tang;P. Sepulveda;J. Marciniszyn;K. C. Chen;W. Huang;N. Tao;D. Liu;J. Lanier
中科院分区：
文献类型：
--
作者：
J. Tang;P. Sepulveda;J. Marciniszyn;K. C. Chen;W. Huang;N. Tao;D. Liu;J. Lanier
作为几年实验的结晶，我们提出了猪胃蛋白酶的完整氨基酸序列，这种酶在一条多肽链中含有 327 个氨基酸残基。在序列测定中，用溴化氰处理酶。纯化了五个所得片段。其中四个片段的氨基酸序列占290个残基。由于 37 个残基羧基末端片段的结构已知，因此未对其进行研究。这些片段的比对是根据我们之前报道的甲硫氨酰肽的序列确定的。我们还发现了活性位点天冬氨酰残基的位置，以及三个二硫桥的配对。商业结晶胃蛋白酶的少量成分被发现在分子的氨基末端含有两个额外的氨基酸残基，Ala-Leu-。这种次要成分显然源自猪胃蛋白酶原激活期间的不同裂解位点。
As the culmination of several years of experiments, we propose a complete amino-acid sequence for porcine pepsin, an enzyme containing 327 amino-acid residues in a single polypeptide chain. In the sequence determination, the enzyme was treated with cyanogen bromide. Five resulting fragments were purified. The amino-acid sequence of four of the fragments accounted for 290 residues. Because the structure of a 37-residue carboxyl-terminal fragment was already known, it was not studied. The alignment of these fragments was determined from the sequence of methionyl-peptides we had previously reported. We also discovered the locations of activesite aspartyl residues, as well as the pairing of the three disulfide bridges. A minor component of commercial crystalline pepsin was found to contain two extra amino-acid residues, Ala-Leu-, at the amino-terminus of the molecule. This minor component was apparently derived from a different site of cleavage during the activation of porcine pepsinogen.