In GH3 rat pituitary tumor cells, VIP bound a single class of high affinity sites with a KD of 17 nM, a higher affinity than PHI (275 nM) or GHRF (1380 nM).
In plain wordsIn rat pituitary tumour cells in culture, VIP bound its receptor more tightly than PHI or GHRF did.
- Outcome
- Not applicableVIP binding affinity (KD) on GH3 cells
- Study
ratn: not reported in source
GH3 rat pituitary tumor cell line- Comparator
- PHI and human pancreatic GHRF
- Outcome group
- Receptor activity and mechanism · Endocrine and hormones
- Studied dose
- Dose not stated
Measurements
- KD
- 17 nM
- VIP, GH3 cells
Source sentences
Studies using 125I-VIP and unlabeled competing peptides revealed a single class of high affinity binding sites with a dissociation constant (KD) of 17 +/- 2 nM (mean +/- S.E.M.) for VIP, 275 +/- 46 nM for peptide histidine isoleucine (PHI), and 1380 +/- 800 nM for human pancreatic growth hormone rel…
1 context sentence(design, population, supporting numbers)
The vasoactive intestinal polypeptide (VIP) receptor was characterized on the GH3 rat pituitary tumor cell line using competitive binding studies with peptides having sequence homology with VIP.