Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UNIPROT:P02749 (
beta2-glycoprotein I
)
836
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Washed human platelets were preincubated with 0-300 micrograms/ml human
beta 2-glycoprotein I
and the effect of this on the adenylate cyclase activity (EC.4.6.1.1.) was studied. Adenylate cyclase activity could be increased 2-3 fold. The same degree of activation was seen when low concentrations of prostaglandin E1 (1 microM) had been present concomitant with
beta 2-glycoprotein I
during preincubation. The dose-response curves of the adenylate cyclase activity measured as a function of the
beta 2-glycoprotein I
concentration were S-shaped in the absence of prostaglandin E1 and hyperbolic in its presence. The results suggest a biological function of
beta 2-glycoprotein I
as a compound conserving and activating the
membrane-bound
adenylate cyclase.
...
PMID:Effect of beta 2-glycoprotein I on the activity of adenylate cyclase in platelet membranes. 668 48
Apolipoprotein H
(
ApoH
) is a plasma glycoprotein with its in vivo physiological and pathogenic roles being closely related to its interaction with negatively charged membranes. In this paper, the interaction of
ApoH
with phospholipid vesicles was characterized by (i) detecting the wavelength shift of the fluorescence spectrum of
ApoH
and (ii) measuring the fluorescence quenching extent of
ApoH
by the membrane resident quencher 1-palmitoyl-2-stearoyl-(5-doxyl)-sn-glycero-3-phosphocholine (DPC). The observed blue shift upon addition of DMPG vesicles indicated that the tryptophan residues of
ApoH
moved from a polar to a nonpolar environment. The insertion ability of
ApoH
into PG-containing vesicles did not depend on the PG content in a stoichiometric way as did the blue shift, indicating that the negatively charged DMPG does not serve as a specific binding site but rather provides a suitable microenvironment for
ApoH
interaction. The finding that the detachment effect of cations on the blue shift is remarkably different from that on the quenching extent suggests that
ApoH
is capable of existing in two different conformations when
membrane-bound
.
...
PMID:Intrinsic fluorescence study of the interaction of human apolipoprotein H with phospholipid vesicles. 1041 25
