Characterization and solubilization of cyclo(His-Pro) binding from rat liver membranes.
We have found cyclo(His-Pro) binding in rat liver plasma membranes. This study focused on the characterization of solubilized binding for cyclo(His-Pro) in rat liver membranes. The cyclo(His-Pro) binding of liver membranes was solubilized by digitonin and octyl-glucopyranoside. The efficiency of solubilization with digitonin was greater. However, cyclo(His-Pro) binding was not solubilized by Triton X-100, CHAPS, or Lubrol. Digitonin-solubilized membranes showed cyclo(His-Pro) binding with a high affinity constant (17 nM) and a low binding capacity (38 fmol/mg protein). Lectins from wheat germ, Bandeiraea simplicifolia II, Dolichos biflorus, Glycine max, and Tetragonolobus purpureas significantly adsorbed [3H]cyclo(His-Pro)-binding complex, but Bandeiraea simplicifolia I, Ricinus communis I, or Lens culinaris did not adsorb the binding complex. An analysis of [3H]cyclo(His-Pro)-associated membranes by high performance gel filtration chromatography showed a radioactive peak of Mr 200,000. These data indicate that cyclo(His-Pro) binding of rat liver membranes is solubilized by digitonin and is a glycoprotein of Mr 200,000.
Mori
M
M
First Department of Internal Medicine, Gunma University, School of Medicine, Maebashi, Japan.
Yamada
M
M
Iriuchijima
T
T
Murakami
M
M
Kobayashi
S
S
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D002850:Chromatography, Gel; D003902:Detergents / Q000494:pharmacology; D037102:Lectins / Q000494:pharmacology; D008099:Liver / Q000378:metabolism* / Q000648:ultrastructure; D008297:Male; D010456:Peptides, Cyclic / Q000378:metabolism*; D010879:Piperazines / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D012995:Solubility
D003902:Detergents; D037102:Lectins; D010456:Peptides, Cyclic; D010879:Piperazines; C015924:histidyl-proline diketopiperazine