Studies on swine and canine serum haptoglobins

Autor: Bong-Sop Shim, Chang-Soo Yoon, Sae-Kun Oh, Tong-Ho Lee, Yoon-Se Kang
Rok vydání: 1971
Předmět:
Zdroj: Biochimica et Biophysica Acta (BBA) - Protein Structure. 243:126-136
ISSN: 0005-2795
DOI: 10.1016/0005-2795(71)90046-8
Popis: Swine and canine serum haptoglobins (Hp) were purified, and their biochemical and immunological properties were investigated and compared with human type 1-1 Hp. The solubilities of swine and canine serum Hp's in (NH4)2SO4 were slightly higher than that of human Hp. The electrophoretic mobilities of both canine and swine Hp-Hb complexes were faster than that of human type 1-1 Hp on starch gel. On the other hand, their immunoelectrophoretic mobilities were slightly slower than these of human type 1-1 Hp both in the free and Hb-complexed states. The retardation of mobility of swine Hp brought about by formation of complexes with Hb was not as pronounced as with canine and human type 1-1 Hp's. Swine and canine Hp's also formed the so-called Hp-Hb intermediate. The urea—starch-gel electrophoretic pattern of swine haptoglobin was similar to that of human type 1-1 Hp, while the mobility of canine α chain was very much slower than those of swine and human α chains. The subunit structures of swine and canine Hp's, and the compositions of swine and canine Hp-Hb intermediate and Hp-Hb complexes were similar to those of human type 1-1 Hp. Some antigenic determinants of swine and canine Hp's were masked by Hb binding, and they also bound with Hb at the β chain like human Hp's.
Databáze: OpenAIRE