Specific high-affinity binding protein for human corticotropin-releasing hormone in normal human plasma

1987 ◽  
Vol 143 (2) ◽  
pp. 411-417 ◽  
Author(s):  
David N. Orth ◽  
Charles D. Mount
Keyword(s):  
Human Plasma ◽  
Binding Protein ◽  
Affinity Binding ◽  
Corticotropin Releasing Hormone ◽  
Normal Human Plasma ◽  
High Affinity Binding ◽  
Releasing Hormone ◽  
High Affinity ◽  
Normal Human

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.

scholarly journals Agrin Is a High-affinity Binding Protein of Dystroglycan in Non-muscle Tissue

1998 ◽  
Vol 273 (1) ◽  
pp. 600-605 ◽  
Author(s):  
Matthias Gesemann ◽  
Andrea Brancaccio ◽  
Beat Schumacher ◽  
Markus A. Ruegg
Keyword(s):  
Muscle Tissue ◽  
Binding Protein ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
High Affinity

A gonadotropin-releasing hormone type neuropeptide with a high affinity binding site for copper(ii) and nickel(ii)

Metallomics ◽  
2019 ◽  
Vol 11 (2) ◽  
pp. 404-414 ◽  
Author(s):  
Kevin K. Tran ◽  
Bhawantha M. Jayawardena ◽  
Maurice R. Elphick ◽  
Christopher E. Jones
Keyword(s):  
Binding Site ◽  
Gonadotropin Releasing Hormone ◽  
Affinity Binding ◽  
Asterias Rubens ◽  
High Affinity Binding ◽  
Releasing Hormone ◽  
High Affinity ◽  
Evolutionarily Conserved ◽  
High Affinity Site ◽  
High Affinity Binding Site

Gonadotropin releasing hormone from Asterias rubens binds Cu(ii) in a nitrogen-rich, high-affinity site. Cu(ii)-binding is an evolutionarily conserved feature of GnRH-type neuropeptides.

Glucocorticoids Decrease a Binding of Corticotropin-Releasing Hormone-Binding Protein in Human Plasma*

1990 ◽  
Vol 71 (4) ◽  
pp. 913-917 ◽  
Author(s):  
TOSHIHIRO SUDA ◽  
TAKASHI SUMITOMO ◽  
YORIKO NAKANO ◽  
FUMIKO TOZAWA ◽  
TSUYAKO USHIYAMA ◽  
...  
Keyword(s):  
Human Plasma ◽  
Binding Protein ◽  
Corticotropin Releasing Hormone ◽  
Hormone Binding ◽  
Releasing Hormone ◽  
Hormone Binding Protein

scholarly journals N-Acylethanolamine Signaling in Tobacco Is Mediated by a Membrane-Associated, High-Affinity Binding Protein

2003 ◽  
Vol 131 (4) ◽  
pp. 1781-1791 ◽  
Author(s):  
Swati Tripathy ◽  
Kathryn Kleppinger-Sparace ◽  
Richard A. Dixon ◽  
Kent D. Chapman
Keyword(s):  
Binding Protein ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
High Affinity

RAT MYOMETRIAL ACTIVITY IN VIVO: EFFECTS OF OESTRADIOL-17β AND PROGESTERONE IN RELATION TO THE CONCENTRATIONS OF CYTOPLASMIC PROGESTERONE RECEPTORS

1978 ◽  
Vol 78 (1) ◽  
pp. 103-117 ◽  
Author(s):  
SANDRA J. DOWNING ◽  
S. J. LYE ◽  
JANE M. C. BRADSHAW ◽  
D. G. PORTER
Keyword(s):  
Binding Protein ◽  
Progesterone Receptors ◽  
Affinity Binding ◽  
Pregnant Rats ◽  
Pregnant Rat ◽  
High Affinity Binding ◽  
High Affinity ◽  
Repeated Doses ◽  
In Vivo Effects

The amplitude, frequency and rate of rise of intra-uterine pressure cycles in rats (postpartum, ovariectomized) were unaffected by treatment with progesterone. Amplitude was also unaffected by a combination of treatments with progesterone and oestradiol-17β, which was adequate to ensure the survival of 84% of foetuses in ovariectomized pregnant rats. The failure of progesterone to influence myometrial activity could not be attributed to a lack of 'true' progesterone receptors since these were present in the myometria of the test animals in concentrations exceeding those of oestrous animals. Evidence was obtained which suggested that a high-affinity binding protein, different from the 'true' receptor may predominate in the myometrium of the pregnant rat. Oestradiol-17β in single or repeated doses of from 0·25 to 5 μg, however, was found to reduce the frequency of pressure cycles but to increase significantly their rate of rise of pressure. There was a latency of 6–8 h in these effects of oestradiol. The possibility that inhibition of the myometrium by oestrogen may play a part in the preparation for parturition is discussed.

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