High-performance liquid chromatography of amino acids, peptides and proteins : LXXV. Isolation of isohormones of bovine thyrotropin and lutropin
โ Scribed by Peter G. Stanton; Milton T.W. Hearn
- Book ID
- 104145839
- Publisher
- Elsevier Science
- Year
- 1987
- Tongue
- English
- Weight
- 879 KB
- Volume
- 397
- Category
- Article
- ISSN
- 1873-3778
No coin nor oath required. For personal study only.
โฆ Synopsis
Purification of bovine thyrotropin and lutropin by conventional soft-gel chromatographic methods is shown to yield microheterogeneous products. High-performance ion-exchange chromatography (HPIEC) can be used to purify these isohormones further for investigations into the structure/function role of glycoprotein microheterogeneity. Hormonal microheterogeneity is shown to be reflected in differences in surface-accessible charged groups, as demonstrated by HPIEC, and differences in net charge, as indicated by isoelectric focusing. Optimal separation of the glycoprotein hormones, based on protein charge, can therefore be achieved by a combination of these two methods.
๐ SIMILAR VOLUMES
The separation of several immunologically related forms of the bovine brain basic heparin-binding growth factor by reversed-phase high-performance liquid chromatography is described. With Bakerbond C4 reversed-phase columns, it is possible to resolve the 0.8-1.0 M sodium chloride and the 1.0-1.3 M s
Cardiodilatin (CDD), a polypeptide exhibiting vasorelaxant and diuretic natriuretic bioactivity, was isolated from bovine atria. The isolation procedure reported here is different from that originally used for the purification of porcine and bovine CDD. Instead of cation-exchange chromatography on F