Studies on the reduction of elastin. II. Evidence for the presence of alpha-aminoadipic acid delta-semialdehyde and its aldol condensation product.
Studies on the reduction of elastin. II. Evidence for the presence of alpha-aminoadipic acid delta-semialdehyde and its aldol condensation product.
复制标题
弹性蛋白减少的研究。
DOI：
10.1021/bi00835a022
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发表时间：
1969
期刊：
影响因子：
2.9
通讯作者：
C. Franzblau
中科院分区：
文献类型：
--
作者：
R. Lent;B. Smith;L. Salcedo;B. Faris;C. Franzblau
RW Lent，B.Smith，LL Salcedo，B.Paris，和C.Franzblau f摘要：关于用硼三钠还原弹性蛋白的研究表明：(1)在用硼三钠还原弹性蛋白的酸性水解物中，大多数氚化合物来自肽链骨架上的修饰赖氨酸残基。从组织培养的鸡胚主动脉中获得的[14C]赖氨酸标记弹性蛋白的研究证实了这一点。(2)弹性蛋白中某些赖氨酸的e-氨基脱氨基形成的a-氨基己二酸-半醛残基被硼氢化钠还原为e-羟基去亮氨酸残留物。还原的弹性蛋白在6nHCl中的水解导致e-羟基去甲亮氨酸的亚基转化为e-氯代亮氨酸，后者在稀碱处理后又转化为吡喃甲酸。对纯e-羟基亮氨酸的研究证实了这些结果。另外，Partridge等人(1966)和Miller等人(1964)明确提出，赖氨酸是弹性蛋白中桥连素和异桥桥素交联链的前体。最近，Franzblau等人(1965)描述了另一种氨基酸，赖氨酸亮氨酸，存在于弹性蛋白的水解物中。这种化合物的结构表明，它也可以作为弹性蛋白的交联剂。我们推测赖氨酸亮氨酸的前体也是赖氨酸。关于硼三钠还原牛弹性蛋白的研究表明，亮氨酸的合成可能是通过形成Schiff碱，6，7-脱氢亮氨酸(Lent and Franzblau，1967)。这可能是由一个氨基己二酸半醛残基和一个赖氨酸残基缩合而成的。除了加入赖氨酸或亮氨酸的组份外，还在马萨诸塞州波士顿波士顿大学医学院生物化学系的几个组分中发现了大量的氚。1969年1月2日收到。这项研究得到了美国国立卫生研究院(AM-07697)和美国心脏协会(65-G-129)的资助。本文提供的数据部分取自RWL.、B.S.和LLS.在部分满足哲学博士学位要求时提交给波士顿大学的论文。RW L.感谢美国国立卫生研究院博士前奖学金。GM-36714。
RW Lent, B. Smith, LL Salcedo, B. Paris, and C. Franzblau f abstract: Studies on the reduction of elastin with sodium borotritide have shown:(1) Most of the tritiated compounds in an acid hydrolysate of elastin previously reduced with so-dium borotritide arise from modified lysine residues in the backbone of the peptide chains. This was confirmed by studies on [14C] lysine-labeled elastin obtained from chick embryo aortas grown in tissue culture.(2) Residues of a-aminoadipic acid-semialdehyde which are formed bythe deamination of the e-amino groupof certain lysineresidues in elastin, are re-duced by sodium borohydride to e-hydroxynorleucine resi-dues. Hydrolysis of reduced elastin in 6 n HC1 leads to sub-stantial conversion of the e-hydroxynorleucine into e-chloronorleucine, which in turn is converted into pipecolicacid upon treatment with dilute alkali. Studies on pure e-hydroxynor-leucine confirmed these results. It was also found that e-hy-11 has been clearly established by Partridge et al.(1966) and Miller et al.(1964) that lysine is the precursor of the desmosine and isodesmosine cross-links in elastin. Recently, Franzblau et al.(1965) described another amino acid, lysinonorleucine, occurring in hydrolysates of elastin. The structure of this com-pound indicates that it too may serve as a cross-linking agent in elastin. We suggested that the precursor of lysinonorleucine also is lysine. Studies on the reduction of bovine elastin with sodium borotritide led to the proposal that synthesis of ly-sinonorleucine probably occurs via formation of the Schiff base, 6 7-dehydrolysinonorleucine (Lent and Franzblau, 1967). This could arise from the condensation of one residue of-aminoadipic acid-semialdehyde and one residue of ly-sine. In addition to that incorporated into the lysinonorleucine fractions, significant amounts of tritium were found in several* From the Department of Biochemistry, Boston University School of Medicine, Boston, Massachusetts. Received January 2, 1969. This research was supported by grants from the National Institutes of Health (AM-07697) and American Heart Association (65-G-129). The data presented in this paper are taken in part from the dissertations of RW L., B. S., and LL S. submitted to Boston University in partial fulfill-ment of the requirements of the degree of Doctor of Philosophy. RW L. is grateful for the National Institutes of Health Predoctoral Fellow-ship No. GM-36714.