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A Salas-Valdés

Publications and source records attributed to A Salas-Valdés.

5 recordsLinked to original sources
PubMed1981

Human pituitary hormones extraction.

In order to know the efficiency of the human pituitary hormone extraction method utilized in the laboratory, six batches of 100 pituitaries each, were collected in acetone. Its delipidization and the initial acid extraction (0.3 M KCl, pH 5.5) of the powder were performed in the presence of 0.1 per cent thioethanol and the extraction was completed with an alkaline solution (0.1 N NaOH + H2O, v/v, pH 10.5). Hields in weight of powder and protein concentration for each fraction were similar to those previously reported by Elrick. Characterization of fractions with disc-gel-electrophoresis demonstrated a reproducible pattern for GH, and some differences among the samples containing the glycoproteins. The hormonal activities determined by radioimmunoassay showed a low contamination of GH in the fractions rich in glycoproteins, but these latter were similarly distributed between the acid and the alkaline extracts. The glycoprotein fraction had an important activity of TSH. The hormonal content per pituitary was calculated from the addition of activities in both extracts and the last residue; GH = 3 mg (4.494 IU); FSH = 761 micrograms (13.410 IU); LH = 782 micrograms (46.920 IU); TSH = 2.939 mg (9.350 IU). It is concluded that the technique is useful since there was a low GH contamination in the glycoprotein fraction and the TSH yield was important.

Electrophoresis, Disc↗
PubMed1979

Polyacrilamide gel electrophoretic pattern of umbilical cord and maternal sera.

A comparative study was performed of the polyacrylamide gel electrophoretic patterns of proteins in 100 sera from the umbilical cord and maternal sera after normal pregnancies and deliveries. To simplify this analysis, the electrophoretic pattern was arbitrarily divided into nine regions that were studied according to the number of band frequency and colour intensity. Protein nomination was made with literature data. Total protein concentrations in both sera were determined by colorimetric techniques. The most important data obtained from umbilical cord serum pattern were the following: a greater number of bands in the post albumin, post beta and gamma 1 regions; absence of "hemopexin" band or faintly stained if present; abundance of 7s-globulins with lack or scarcity of "haptoglobin" bands in gamma 2 region in 100 per cent of gels; and finally, the band closer to the origin (B-lipoprotein) slightly stained. Minimum number of bands was 11, maximum 24. Features of maternal serum were: highly stained "hemopexin" in 100 per cent of gels; frequent band absence in gamma 1 region; in gamma 2 region, there are scarce 7s globulins and "haptoglobins" are numerous and highly stained; in the middle part of this same region, frequent presence of a band that is more coloured than "haptoglobins"; the three last bands close to the origin are always observed showing high staining. Minimum number of bands was 13 and maximum 30. Total protein average concentration was 6.28/g/100 ml in umbilical cord serum and 7.14/g/100 ml in mother serum. Comparison of electrophoretic patterns in 100 paired sera showed that only three were identical. In this paper we discuss some of the possible causes of differences observed between both sera.

Blood Protein Electrophoresis↗