TY  - JOUR
A1  - Jaenicke, Rainer
A1  - Pavlíček, Zdeněk
T1  - On the nature of the hemoglobin-haptoglobin interaction
T2  - Zeitschrift für Naturforschung, B
N2  - The interactions between human haptoglobin, Hp II (genetic types 2 - 1 and 2-2), and bovine hemoglobin, Hb, were investigated taking inhibition of complex formation and complex dissociation in various solvent media as criteria.
As shown by relative peroxidase activity and gel chromatography, complex dissociation occurs at high concentrations of guanidine HCl, urea, sodium chloride, dioxane, and formaldehyde, while in case of sodium dodecylsulfate a low molar ratio (SDS/Hb -Hp<5) is sufficient to split the complex. In general the formation of the complex stabilizes the structure of its constituents.
Excluding solvent conditions which lead to denaturation (as measured by optical rotation), ionpairs and H-bonds seem to prevail in the stabilization of the complex, while hydrophobic interactions should be of minor importance. Chemical modification of histidine and tyrosine with diazonium-1-H-tetrazole and N-acetylimidazole, respectively, prove histidyl-groups in Hb and tyrosylgroups in Hp to participate in the Hb-Hp contact, thus confirming earlier results.
Y1  - 2014
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/71468
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-714682
SN  - 1865-7117
SN  - 0932-0776
VL  - 25
IS  - 11
SP  - 1272
EP  - 1277
PB  - Verlag der Zeitschrift für Naturforschung
CY  - Tübingen
ER  -