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PubMed1985

Effect of aging on human aortic protein composition. I. One-dimensional polyacrylamide gel electrophoretic analysis of tissue extracts.

Proteins extracted from matching areas of homogenized intimas of 17 human aortas, from two age groups (15-34 and 35-82), were studied after separation by polyacrylamide gel electrophoresis, silver staining, and densitometric scanning. Several definite protein bands including 6 major and 16 minor bands were identified in 17 aortic intima samples grossly and microscopically lesion free. However, such electrophoretic patterns were found to differ in the two age groups studied. For instance, (1) the integrated densities (amounts) of protein bands 1, 6, 13, 16, and 19 which we interpreted as of mural vascular origin were significantly higher in the younger age group, whereas the amounts of bands 2, 7, 9, 11, and 21 suspected to be of plasma origin were found to be significantly higher in the older age group; (2) protein band No. 8 was found to be double in the younger age group vs a single line in the older age group, whereas band No. 12 was the opposite. These changes in protein composition appear to correlate closely with diffuse intimal thickening found histologically in older age group, and will be further studied to relate to those in atherosclerotic lesions.

Adolescent↗
PubMed1986

Basic proteins in the human aortic intima: nonequilibrium two-dimensional electrophoretic analysis of tissue extracts.

The protein composition of atheroma-free human thoracic intima was compared with that containing fatty streaks or fibro-fatty lesions utilizing two-dimensional gel electrophoresis (2-DE) and silver staining. Intimal proteins extracted with 9 M urea were separated by nonequilibrium pH gradient electrophoresis (NEPHGE) followed by polyacrylamide gel electrophoresis (PAGE) in the second dimension. NEPHGE-PAGE of proteins extracted from atheroma-free intima revealed several major proteins: actin, tropomyosin-like proteins, proteins with relative molecular weight (Mr) of 250,000 (P250), two proteins with Mr about 15,000 (P15a, P15b), and many medium proteins such as a myosin heavy chain, two myosin light chains, and proteins P47, P44, P32, P27, P20a, P20b, P19a, P19b. Several additional proteins were observed in intimas with fatty streaks and fibro-fatty lesions. Most of them, such as albumin, transferrin, Apo A-I, alpha 1-antitrypsin, fibrinogen beta-chain, IgG, appear to originate from plasma. Differences in protein composition of intima with fibro-fatty streaks compared with adjacent lesion-free intima varied from case to case and need further study. NEPHGE-PAGE in combination with isoelectric focusing (ISO)-PAGE revealed more intimal proteins in atheroma-free and diseased aortas than either method alone, proteins which might be quantitated, isolated for binding studies, and further evaluated for their potential role in atherogenesis.

Actins↗
PubMed1987

Effect of molybdenum treatments on the distribution of Cu and metallothionein in tissue extracts from rats and sheep.

An examination was made of the effects of tetrathiomolybdate (TTM), ammonium molybdate (AM), sodium sulphide, and two molybdo amino acids (cysteine-Mo, cysteine-Mo-S) on the distribution of Cu and Zn among proteins in extracts of the livers and kidneys of rats and sheep. Tetrathiomolybdate caused a shift in the chromatographic distribution of Cu from low molecular weight proteins such as metallothionein (MT) to proteins of higher molecular weight (greater than 100,000 daltons). This was not due to polymerization or cross-linking of metallothionein with the latter, but to the formation of protein-TTM complexes that had a strong affinity for Cu. There was a concomitant redistribution of Zn towards proteins of low molecular weight. Pretreatment of high molecular weight proteins from rat liver with TTM greatly increased the capacity of the proteins to remove Cu from MT. When AM or sodium sulphide were added together to extracts of rat liver, changes similar to those induced by TTM were observed in the chromatographic distribution of Cu and Zn. Individually, these compounds had no significant effect on the distribution of the metals. Of the two molybdo amino acids, only cysteine-Mo-S altered the chromatographic distribution of Cu in extracts of rat liver. The redistribution was in the same direction as that induced by TTM, but was not as pronounced.

Animals↗
PubMed1985

Chemoreceptively active compounds in secretions, excretions and tissue extracts of marine mammals.

Semen, prostate glandular extract, perianal glandular secretion, urine, feces and blood from Atlantic bottlenose dolphins, Tursiops truncatus, were analyzed chemically by gas chromatography. A fecal sample from a California sea lion, Zalophus californianus, was analyzed similarly. Acids, esters, amino acids, amines, steroids, esters, sugars and alcohols were among the compounds revealed in the analyses. Twenty-two identified compounds can be detected gustatorily in aqueous solutions of sufficient concentration by humans. The chemical compositions of samples from Tursiops are similar to those from humans and other mammals.

Ammonia↗
PubMed1987

In vitro hatching of the infective eggs of Ascaridia galli in tissue extracts.

Extracts of proventriculus (PE) and small intestine (IE) of fowl were used, for the first time, as media for the in vitro hatching of infective eggs of Ascaridia galli. Hatching was successful in a mixture of equal parts of PE and IE (MIP) under normal air and under different concentrations of CO2, but not under 100% CO2. A very highly significant retardation (P less than 0.001) in the rate of hatching appeared as the concentration of CO2 was increased, indicating that high levels of CO2 inhibit the process of hatching. 100% of the eggs hatched in PE in 40.5 min whereas they did not hatch at all in IE, suggesting that IE alone has no influence on egg hatching. The shortest time taken for 100% of the eggs to hatch in this study suggests that the present method of hatching is faster than all previous methods used by different workers.

Animals↗