| Popis: |
Highly purified porcine and bovine luteinizing hormone subunits, LHα and LHβ, have been chromatographed on agarose gel in 6 m guanidine HCl. All nonreduced subunits gave essentially one symmetrical peak, as did reduced bovine LHα and LHβ. In contrast, reduced porcine LHα and LHβ gave three and two peaks, respectively. It is proposed that, whereas bovine LHα and LHβ are single chain proteins, each of the porcine subunits consists of two populations of molecules, one with single peptide chains and the other with two peptide chains linked by disulfide bonds. |
