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胰岛素的硫醇化和二硫键交联以形成具有潜在治疗价值的大分子。

Thiolation and disulphide cross-linking of insulin to form macromolecules of potential therapeutic value.

作者信息

Mahbouba M, Smith H J

出版信息

Adv Exp Med Biol. 1977;86A:247-60. doi: 10.1007/978-1-4684-3282-4_15.

DOI:10.1007/978-1-4684-3282-4_15
PMID:920500
Abstract

Macromolecules have been prepared containing native insulin carried by a modified insulin skeleton made by partially thiolating the insulin hexamer and forming intermolecular cross-links through disulphide bridges. Oxidation of partially thiolated insulin (0.5-0.7 SH group/mole), formed by reacting insulin with AHTL, with, (a) potassium ferricyanide, (b) Cu++-oxygen gave water soluble macromolecules containing 20-26 and 410-708 monomer units respectively which had rod-random coil shape (light scattering). The larger molecules formed by (b) contained 8g-atom CU++/hexamer unit and insulin. The insulin was firmly bound within the marcomolecules and was probably bound within an insulin-modified insulin hexamer through coordination to copper.

摘要

已经制备了大分子,其包含由修饰的胰岛素骨架携带的天然胰岛素,该修饰的胰岛素骨架通过部分硫醇化胰岛素六聚体并通过二硫键形成分子间交联而制成。通过使胰岛素与AHTL反应形成的部分硫醇化胰岛素(0.5 - 0.7个巯基/摩尔)与(a)铁氰化钾、(b)Cu²⁺ - 氧气氧化,分别得到含有20 - 26个和410 - 708个单体单元的水溶性大分子,其具有棒状 - 无规卷曲形状(光散射)。由(b)形成的较大分子含有8克原子Cu²⁺/六聚体单元和胰岛素。胰岛素牢固地结合在大分子内,并且可能通过与铜配位而结合在胰岛素修饰的胰岛素六聚体内。

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Thiolation and disulphide cross-linking of insulin to form macromolecules of potential therapeutic value.胰岛素的硫醇化和二硫键交联以形成具有潜在治疗价值的大分子。
Adv Exp Med Biol. 1977;86A:247-60. doi: 10.1007/978-1-4684-3282-4_15.
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引用本文的文献

1
Insulin aggregation in artificial delivery systems.
Diabetologia. 1980 Jul;19(1):1-9. doi: 10.1007/BF00258302.
2
The fate of insulin in cardiac muscle. Studies on isolated muscle cells from adult rat heart.胰岛素在心肌中的命运。对成年大鼠心脏分离的肌肉细胞的研究。
Biochem J. 1982 Sep 15;206(3):655-62. doi: 10.1042/bj2060655.
3
Insulin degradation by adipose tissue. Studies at several levels of cellular organization.脂肪组织对胰岛素的降解。细胞组织多个层面的研究。
Biochem J. 1980 Jan 15;186(1):351-60. doi: 10.1042/bj1860351.