生物
酪氨酸酶
核酸序列
肽序列
分子生物学
生物化学
序列分析
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细胞外
埃德曼退化
葡聚糖
结构基因
基因
突变体
酶
作者
Valerie S. Bernan,David Filpula,Wayne K. Herber,Mervyn J. Bibb,Edward Katz
出处
期刊:Gene
[Elsevier]
日期:1985-01-01
卷期号:37 (1-3): 101-110
被引量:171
标识
DOI:10.1016/0378-1119(85)90262-8
摘要
The sequence of a 1.56-kb DNA fragment containing the tyrosinase gene (mel) from Streptomyces antibioticus was determined and the Mr (30612) and amino acid (aa) sequence of the protein were deduced from the nucleotide (nt) sequence. Intracellular and extracellular tyrosinase from S. antibioticus, transformed with pIJ702 (containing mel), were purified to homogeneity; the Mr (29500), as determined by Sephadex G-75 chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), was consistent with the value derived from the nt sequence. Edman degradation established that the N-terminal sequence of both the intracellular and extracellular forms of tyrosinase are identical and correspond to the aa sequence derived from the structural gene. In addition, this sequence exhibits striking homology to the N-terminal region of the intracellular and extracellular enzyme purified from Streptomyces glaucescens (Crameri et al., 1982). An additional open reading frame (ORF438) upstream of the mel gene, was also identified that appears to code for a protein (Mr = 14754) with a putative signal sequence.
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