Characterization of hepta-β-glucoside elicitor-binding protein(s) in soybean

1994 ◽  
Vol 22 (2) ◽  
pp. 408-414 ◽  
Author(s):  
Michael G. Hahn ◽  
Jong-Joo Cheong ◽  
Rob Alba ◽  
François Côté
Keyword(s):  
Binding Protein ◽  
Protein S

scholarly journals Characterization of a Putative Insulin-Responsive Element and Its Binding Protein(s) in Rat Angiotensinogen Gene Promoter: Regulation by Glucose and Insulin*

Endocrinology ◽  
2001 ◽  
Vol 142 (6) ◽  
pp. 2577-2585 ◽  
Author(s):  
Xing Chen ◽  
Shao-Ling Zhang ◽  
Li Pang ◽  
Janos G. Filep ◽  
Shiow-Shih Tang ◽  
...  
Keyword(s):  
Binding Protein ◽  
Gene Promoter ◽  
Protein S ◽  
Promoter Regulation ◽  
Angiotensinogen Gene ◽  
Responsive Element

Characterization of imidazoline binding protein(s) solubilized from human brainstem: Studies with [3H]idazoxan and [3H]clonidine

1994 ◽  
Vol 25 (2) ◽  
pp. 183-191 ◽  
Author(s):  
Hugues Greney ◽  
Giampiero Bricca ◽  
Monique Dontenwill ◽  
Jeanne Stutzmann ◽  
Pascal Bousquet ◽  
...  
Keyword(s):  
Binding Protein ◽  
Protein S

Characterization of V3 Loop-Binding Protein(s) of Molt-4 and U937 Cells

1995 ◽  
Vol 11 (5) ◽  
pp. 563-570 ◽  
Author(s):  
YOUNONG XU ◽  
TOSHIO MURAKAMI ◽  
SHIDO KAWASE ◽  
TAKASHI UCHIYAMA ◽  
TOSHIO HATTORI
Keyword(s):  
Binding Protein ◽  
Protein S ◽  
V3 Loop ◽  
U937 Cells

PARTIAL PURIFICATION AND CHARACTERIZATION OF A BINDING PROTEIN FOR INSULIN-LIKE ACTIVITY (ILAs) IN HUMAN AMNIOTIC FLUID: A POSSIBLE INHIBITOR OF INSULIN-LIKE ACTIVITY

1979 ◽  
Vol 90 (3) ◽  
pp. 505-518 ◽  
Author(s):  
Stenvert L. S. Drop ◽  
Guy Valiquette ◽  
Harvey J. Guyda ◽  
Maité T. Corvol ◽  
Barry I. Posner
Keyword(s):  
Amniotic Fluid ◽  
Binding Protein ◽  
Apparent Molecular Weight ◽  
Protein S ◽  
Radioreceptor Assay ◽  
Partial Purification ◽  
Human Amniotic Fluid ◽  
Biological Assays ◽  
Insulin Like Activity

ABSTRACT An insulin radioreceptor assay (INS-RRA) and an insulin-like activity radioreceptor assay (ILAs-RRA) have been utilized to partially purify and characterize a protein from human amniotic fluid with ILAs-RRA reactivity. An acid-ethanol soluble protein with an apparent molecular weight of 34 500 daltons by calibrated Sephadex chromatography and an isoelectric point (pI) of 4.7 accounts for all of the ILAs-RRA reactivity present in human amniotic fluid. Since this protein has been found to be a binding protein for ILAs. but not for insulin, it has been termed amniotic fluid binding protein or AFBP. AFBP is reactive in a non-parallel manner in the ILAs-RRA and totally inactive in the INS-RRA. The activity of AFBP in the ILAs-RRA is thus to the competition of AFBP with the placental membrane receptor for the [125I]ILAs tracer employed in the ILAs-RRA. AFBP inhibits the activity of added ILAs, but not of added insulin, in the INS-RRA, presumably by binding ILAs, while being inactive itself. In two biological assays studied to date, the rat epididymal fat pad assay and the rabbit chondrocyte sulphation assay, AFBP also inhibits the activity of added ILAs. These observations raise the possibility that binding protein(s) for insulin-like peptides may function as inhibitors of their bioactivity in different physiologic and pathologic states. The relation of AFBP to binding protein(s) in human plasma remains to be clarified.

Plasma Components which Interfere with Ristocetin-induced Platelet Aggregation

1975 ◽  
Vol 33 (03) ◽  
pp. 540-546 ◽  
Author(s):  
Robert F Baugh ◽  
James E Brown ◽  
Cecil Hougie
Keyword(s):  
Platelet Aggregation ◽  
Human Plasma ◽  
Plasma Proteins ◽  
Binding Protein ◽  
Plasma Heating ◽  
Protein S ◽  
Fold Increase ◽  
Normal Human Plasma ◽  
Preliminary Examination ◽  
Normal Human

SummaryNormal human plasma contains a component or components which interfere with ristocetin-induced platelet aggregation. Preliminary examination suggests a protein (or proteins) which binds ristocetin and competes more effectively for ristocetin than do the proteins involved in ristocetin-induced platelet aggregation. The presence of this protein in normal human plasma also prevents ristocetin-induced precipitation of plasma proteins at levels of ristocetin necessary to produce platelet aggregation (0.5–2.0 mg/ml). Serum contains an apparent two-fold increase of this component when compared with plasma. Heating serum at 56° for one hour results in an additional 2 to 4 fold increase. The presence of a ristocetin-binding protein in normal human plasma requires that this protein be saturated with ristocetin before ristocetin-induced platelet aggregation will occur. Variations in the ristocetin-binding protein(s) will cause apparent discrepancies in ristocetin-induced platelet aggregation in normal human plasmas.

Detection and characterization of a heat and acid stable progesterone binding protein in the rat lung

1984 ◽  
Vol 104 (4_Supplb) ◽  
pp. S91-S92
Author(s):  
G. DAXENBICHLER ◽  
E. H. MOSER
Keyword(s):  
Binding Protein ◽  
Rat Lung ◽  
Acid Stable
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