Zobrazeno 1 - 7
of 7
pro vyhledávání: '"J. P. ARCOLEO"'
Publikováno v:
Journal of Biological Chemistry. 258:1227-1234
Selective proteolysis has been used to delineate the hemoglobin-binding site on haptoglobin heavy chain. Haptoglobin was cleaved specifically by plasmin, trypsin, chymotrypsin, staphylococcal protease, and thermolysin. Haptoglobin-hemoglobin complex
Autor:
J P Arcoleo, J Greer
Publikováno v:
Journal of Biological Chemistry. 257:10063-10068
Haptoglobin forms a stable, irreversible complex with hemoglobin. The H chain of haptoglobin, which is the subunit that binds hemoglobin, shows strong sequence homology with the serine protease family. This raises the question of whether hemoglobin b
Publikováno v:
Journal of Biological Chemistry. 256:672-679
Publikováno v:
The Journal of biological chemistry. 258(2)
Selective proteolysis has been used to delineate the hemoglobin-binding site on haptoglobin heavy chain. Haptoglobin was cleaved specifically by plasmin, trypsin, chymotrypsin, staphylococcal protease, and thermolysin. Haptoglobin-hemoglobin complex
Publikováno v:
Chemischer Informationsdienst. 7
Publikováno v:
Chemischer Informationsdienst. 8
Autor:
J P, Arcoleo, J, Greer
Publikováno v:
The Journal of biological chemistry. 257(17)
Haptoglobin forms a stable, irreversible complex with hemoglobin. The H chain of haptoglobin, which is the subunit that binds hemoglobin, shows strong sequence homology with the serine protease family. This raises the question of whether hemoglobin b