Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P61278 (somatostatin)
 22,083 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Somatostatin is widely distributed in tissues of biological fluids. In the present study we tested the validity of a new radioimmunoassay by a solid phase immunoextraction. Sensitivity was 1.8 pg/mL and the within-assay precision with two different pools of human plasma was 12.2% (CV) at a concentration of 19.2 +/- 2.34 pg/mL (mean +/- SD) and 11.9% at 8.53 +/- 1.02 pg/mL. The between assay precision was 14.2% (CV) at a concentration of 11.8 +/- 1.68 pg/mL. The accuracy was good as tested by the dilution test (slope: 0.956, Y-intercept 3.07 pg/mL, r = 0.997) and the recovery test (slope: 1.008, Y-intercept 2.22 pg/mL, r = 0.999). The method resulted in good correlation with a current extraction method (no. 65, y = 1.45 + 0.975 x, r = 0.862, P less than 0.001). Basal value of somatostatin in the plasma of 32 normal subjects was 11.5 +/- 5.80 pg/mL (mean +/- SD).
Int J Rad Appl Instrum B 1988
PMID:Development of a solid phase RIA for human plasma somatostatin. 290 3

In most patients with acromegaly basal serum GH concentrations are elevated and remain above 5 micrograms/L after oral glucose administration. In some patients, however, serum insulin-like growth factor I (IGF-I) concentrations are elevated with only minimal elevations of serum GH. We studied the serum GH and IGF-I of two such patients to determine whether these peptide hormones are normal in this clinical situation. The serum GH of these patients was found to bind normally to receptors of the IM-9 lymphocyte. The elution pattern of IGF-I extracted from the patients' serum was similar to that of (Thr59) human IGF-I after passage through a Bio-Rad P-60 column in 0.5 M acetic acid. The IGF-I was further characterized by isoelectric focusing and C18 reverse phase high pressure liquid chromatography (HPLC). The isoelectric points of the IGF-I components were similar to those of IGF-I in normal serum. The IGF-I in one patient had two components by HPLC, while that of the other patient had only one major component. The IGF-I components isolated by HPLC were normally active in stimulating [3H] alpha-aminoisobutyric acid uptake by normal human fibroblasts. The elevated serum IGF-I concentrations of these two patients were GH dependent. Transsphenoidal adenomectomy in one patient resulted in a decline in serum IGF-I to a high normal concentration. Lowering the serum GH to subnormal concentrations by the administration of the somatostatin analog SMS 201-995 (Sandoz) restored normal IGF-I concentrations in the second patient. We conclude that the GH and IGF-I of these two patients cannot account for their apparent enhanced GH responsiveness.
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PMID:Characterization of serum growth hormone (GH) and insulin-like growth factor I in active acromegaly with minimal elevation of serum GH. 365 10

Analysis of peptides by reverse-phase high-pressure liquid chromatography would be simplified if retention times could be predicted by summing the contribution to retention of each of the peptide's amino acid side chains. This paper describes the derivation of values ("retention coefficients") that represent the contribution to retention of each of the common amino acids and end groups. Peptide retention times were determined on a Bio-Rad "ODS" column at room temperature with a linear gradient from 0.1 M NaclO(4), pH 7.4 or 2.1, at 0 min to 60% acetonitrile/0.1 M NaclO(4) at 80 min. The NaclO(4), a chaotropic agent, was added to improve peak shape and to minimize conformational effects. Retention coefficients for the amino acids were computed by using a Hewlett-Packard 9815A calculator programmed to change the retention coefficients for all amino acids sequentially to obtain a maximum correlation between actual and predicted retention times. Correlations of 0.999 at pH 7.4 and 0.997 at pH 2.1 were obtained for 25 peptides including glucagon, oxytocin, [Met]enkephalin, neurotensin, and somatostatin. This high degree of correlation suggests that, for peptides containing up to 20 residues, retention is primarily due to partition processes that involve all the residues. Although steric or conformational factors do have some effect on retention, the data suggest that under the above chromatographic conditions the retention of peptides containing up to 20 residues can be predicted solely on the basis of their amino acid composition. This possibility was tested by using data taken from the literature.
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PMID:Prediction of peptide retention times in high-pressure liquid chromatography on the basis of amino acid composition. 692 13