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从猪脊髓中分离了两个生物活性肽,并进行了部分鉴定.氨基酸分析、电泳、等电聚焦及N末端残基丹磺酰衍生物层析分析表明,这两个肽都是纯肽.氨基酸组成分析及Sephadex G50(超细)薄层层析测定的表观分子量表明SCP-1是个31肽,SCP-2是个25肽.SCP-1及SCP-2的N末端氨基酸分别为精氨酸及色氨酸。SCP-1刺激离体豚鼠迥肠收缩,SCP-2引起大鼠血压降低,两者均无吗啡样活性。SCP-I及SCP-2的化学组成和生物学性质与迄今发现的所有已知肽不同。
Two bioactive peptides were isolated from porcine spinal cord and partially identified.Amino acid analysis, electrophoresis, isoelectric focusing and N-terminal residue dansyl derivatives chromatography showed that both peptides were pure peptides. The apparent molecular weight of the amino acid composition analysis and Sephadex G50 thin layer chromatography revealed that SCP-1 was a 31-mer peptide and SCP-2 was a 25-mer peptide. The N-terminal amino acids of SCP-1 and SCP-2 were arginine And tryptophan. SCP-1 stimulates contractile contraction of isolated guinea pigs and SCP-2 causes a decrease in blood pressure in rats, both of which exhibit no morphine-like activity. The chemical composition and biological properties of SCP-I and SCP-2 are different from all the known peptides found so far.