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V M Sanchez-Hidalgo

Publications and source records attributed to V M Sanchez-Hidalgo.

2 recordsLinked to original sources

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↗

Polyacrylamide gel electrophoresis in human serum proteins in "normal" individuals and cancer patients.

The electrophoretic pattern of serum proteins of 100 "normal" adults and 97 non treated patients bearing different types of neoplasias were comparatively studied in polyacrylamide gel to find out if there are specific proteins or protein patterns in cancer. Densitometry was used to complete the study so as to analyze quantitative differences for each one of the regions of the arbitrarily divided electrophoregram of both types of sera. Strictly standardized colorimetric technique was used to quantify total proteins. Protein nomenclature was taken from literature data. As an average we found more bands in the cancer bearing patients than in "normal" individuals that also showed greater colour affinity in proteins. In the different regions, the main feature of neoplasia case was the presence of fewer bands in the post albumin (PA) and alpha-beta (post-beta) zones and many in 7s-globulin region (7s-g) than those found in "normals". The most important changes in the electrophoretic pattern of cancer patient serum were: a) Decrease in prealbumin (Pa), albumin (Alb), some from the postalbumin region (PA) and transferrin (T); frequent absence of ceruloplasmin (Cer) and complement factor 3 (C3) in a reduced number of cases. b) Marked increase of one alpha 1 glycoprotein in the PA region, hemopexin, haptoglobins and alpha 2-macroglobulin. Densitometry was useful to improve data obtained from visual analysis of gels but it could not make a quantitative differentiation of changes observed in beta and 7s-g regions. There was no significant difference in total protein concentration. Advantages and limitations of this method are discussed and results obtained are analyzed.

Adolescent↗