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禽类肌肉营养不良中的肌球蛋白重链与新生儿同工酶相对应。

Myosin heavy chain in avian muscular dystrophy corresponds to the neonatal isozyme.

作者信息

Huszar G, Vigue L, Haines J

出版信息

J Biol Chem. 1985 Aug 25;260(18):9957-60.

PMID:3160708
Abstract

We have previously demonstrated, based on comparison of homologous amino acid sequences and of two-dimensional CNBr peptide gel patterns, that the myosin heavy chain in pectoralis muscles of Storrs, Connecticut dystrophic chickens is different from that of their normal controls (Huszar, G., Vigue, L., De-Lucia, J. Elzinga, M., and Haines, J. (1985) J. Biol. Chem. 260, 7429-7434). Others have shown, however, that genomic banks and mRNA complements of the control and dystrophic birds are not different. In the present studies, we have examined the hypothesis that the "dystrophic" myosin heavy chain is not a novel gene product, but is a developmental isozyme which is expressed in pectoralis muscles of adult chickens due to the dystrophic process. Two-dimensional maps of myosin heavy chain CNBr peptides were prepared from breast muscles of 17-day in ovo (embryonic), 25-day posthatch (neonatal), and adult birds of the Storrs dystrophic and of two control strains. Also, myosin and actomyosin ATPase enzymatic activities of the various preparations were determined in the pH range of 5.5 to 9.0. Analysis of the peptide maps demonstrates that the embyronic, neonatal, and control adult myosin heavy chain isozymes are distinctly different gene products with only minute variations between the respective developmental isozymes in dystrophic and control muscles. However, the pectoralis myosin heavy chain of adult dystrophic birds, which is a homogeneous isozyme population by amino acid sequences and gel patterns, corresponds to that of the neonatal-type myosin heavy chain. The ATPase properties of the embryonic, neonatal, or adult pectoralis myosins and actomyosins were not different, whether the level of specific activity or the pattern of pH activation is considered. Since the mobility of neonatal chicks (primarily neonatal-type isozymes) is not restricted, the differences in myosin heavy chain structures are part of the syndrome, but not the cause of avian muscular dystrophy.

摘要

我们之前基于同源氨基酸序列以及二维溴化氰肽图谱的比较证明,康涅狄格州斯托尔斯市的营养不良型鸡胸肌中的肌球蛋白重链与其正常对照鸡的不同(胡萨尔,G.,维格,L.,德卢西亚,J.,埃尔津加,M.,以及海恩斯,J.(1985年)《生物化学杂志》260卷,7429 - 7434页)。然而,其他人已表明,对照鸡和营养不良型鸡的基因组文库及mRNA互补物并无差异。在本研究中,我们检验了这样一个假说,即“营养不良型”肌球蛋白重链并非一种新的基因产物,而是一种发育同工酶,由于营养不良过程而在成年鸡的胸肌中表达。从17日龄的胚胎期、25日龄的孵化后(新生期)以及成年的斯托尔斯营养不良型鸡和两个对照品系的鸡的胸肌中制备了肌球蛋白重链溴化氰肽的二维图谱。此外,还测定了各种制剂在5.5至9.0的pH范围内的肌球蛋白和肌动球蛋白ATP酶活性。对肽图谱的分析表明,胚胎期、新生期以及对照成年期的肌球蛋白重链同工酶是明显不同的基因产物,在营养不良型肌肉和对照肌肉各自的发育同工酶之间仅有微小差异。然而,成年营养不良型鸡的胸肌肌球蛋白重链,按氨基酸序列和凝胶图谱来看属于同质性同工酶群体,与新生型肌球蛋白重链相对应。无论考虑比活性水平还是pH激活模式,胚胎期、新生期或成年期胸肌肌球蛋白及肌动球蛋白的ATP酶特性并无差异。由于新生雏鸡(主要是新生型同工酶)的活动不受限制,肌球蛋白重链结构的差异是该综合征的一部分,但并非禽类肌肉营养不良的病因。

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