SEX DIFFERENCE AND GONADAL HORMONE INFLUENCE ON SYRIAN HAMSTER KIDNEY ESTERASE ISOZYMES

Thirteen esterase isozymes were separated from kidney extracts of normal adult Syrian hamsters ( Mesocricetus auratus) using the zymogram technique with vertical starch gel electrophoresis and naphthyl esters as substrates. The activities of two esterases were altered by gonadectomy and by treatment with testosterone or estradiol-17β but not with progesterone. One of these esterases showed negligible activity in castrated males and in normal and spayed females. The activity of this esterase increased appreciably in castrated males treated with testosterone or estradiol and in testosterone-treated spayed females. This enhanced activity, however, was not consistent in spayed females treated with estradiol. No sex differences in renal esterases were observed in immature hamsters but a variation was detected in normal adults. The difference appears to be of normal enzyme levels rather than the absence of any esterase. Under the influence of estradiol and progesterone, separately or in combination, distinct alterations in kidney esterase profiles were observed. Certain other quantitative hormonal effects were found. These hormone-dependent esterases do not appear to be cholinesterases, as they were unaffected by eserine. The marked sensitivity of various hamster kidney esterases to estrogen appears to be a unique response and may be related to the estrogenic induction of renal adenocarcinoma, initiated under similar conditions, but not found with androgen-treated or other estrogenized animals. These findings indicate that gonadal effects on the hamster kidney may be of a more complex nature than has been considered heretofore.

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Esterase isozyme patterns in Glycine max exposed to gamma radiation

Canadian Journal of Botany ◽

10.1139/b74-034 ◽

1974 ◽

Vol 52 (1) ◽

pp. 273-275 ◽

Cited By ~ 3

Author(s):

José A. Ferrer-Monge

Keyword(s):

Glycine Max ◽

Gamma Radiation ◽

Gel Electrophoresis ◽

Soybean Seed ◽

Starch Gel Electrophoresis ◽

Esterase Isozyme ◽

Esterase Isozymes ◽

Isozyme Patterns ◽

Starch Gel ◽

Naphthyl Acetate

The esterase isozyme patterns for irradiated and non-irradiated soybean seed and seedlings were determined by starch gel electrophoresis. Patterns were determined for cotyledons, hypocotyl, epicotyl, first pair of leaves, and roots. Two different esterase systems, E1 and E2, were detected by using appropriate substrates. E1 produces three anodic bands with both α- and β-naphthyl acetate. E2 acts only on α-naphthyl acetate producing three cathodic bands. Radiation did not change the patterns. Results indicate that esterase isozymes are more abundant in the aerial than in the underground portion of developing seedlings.

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CONGENITAL NONSPHEROCYTIC HEMOLYTIC ANEMIA ASSOCIATED WITH ERYTHROCYTE GLUCOSE-6-PHOSPHATE DEHYDROGENASE DEFICIENCY IN A NEGRO FAMILY

PEDIATRICS ◽

10.1542/peds.37.4.624 ◽

1966 ◽

Vol 37 (4) ◽

pp. 624-629

Author(s):

Aaron Grossman ◽

K. Ramanathan ◽

Parvin Justice ◽

Joan Gordon ◽

Nasrollah T. Shahidi ◽

...

Keyword(s):

Enzyme Activity ◽

Hemolytic Anemia ◽

Gel Electrophoresis ◽

Dehydrogenase Deficiency ◽

Red Cells ◽

Starch Gel Electrophoresis ◽

Negro Family ◽

Starch Gel ◽

Normal Enzyme ◽

Glucose 6 Phosphate Dehydrogenase

This paper describes a Negro family with congenital nonspherocytic hemolytic anemia associated with glucose-6-phosphate dehydrogenase deficiency. All four affected males in this family showed a hemolytic anemia characterized by low hemoglobin, reticulocytosis, and jaundice. There was no detectable G-6-P D in the red cells and about a tenth of normal enzyme activity in the white cells. By starch gel electrophoresis, the G-6-P D was present as a single band which migrated at the rate of 104% of normal. Physico-chemical studies revealed a marked increase of the Michaelis constant for both G-6-P and TPN, a marked lability of the enzyme upon heating at 40°C and 48°C, and a single narrow peak at pH 9.0. Most of these features were similar to those seen in the Oklahoma I variant. Four of the females in the family were studied (two sisters, the mother, and a maternal aunt of the propositus); all showed a lesser degree of anemia and reticulocytosis but no jaundice, except in the mother. There was a decrease of haptoglobins and both the mother and one sister showed a decrease of erythrocyte survival time as measured by chromium-51. The female members had between 11 and 26% of normal G-6-P D activity in the red cells and between 35 and 63% of normal enzyme activity in the white cells. Starch gel electrophoresis in the mother and aunt showed a single band which migrated at 110% of normal with a trail at the position of the affected males. The presence of a milder degree of hemolysis in the heterozygous carriers of the gene for G-6-P D deficiency associated with congenital nonspherocytic hemolytic anemia provides further support for the Lyon hypothesis in man.

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ESTERASE ISOZYMES IN CANADIAN BARLEY CULTIVARS

Canadian Journal of Plant Science ◽

10.4141/cjps72-081 ◽

1972 ◽

Vol 52 (4) ◽

pp. 507-516 ◽

Cited By ~ 9

Author(s):

GEORGE FEDAK ◽

TIBOR RAJHATHY

Keyword(s):

Gel Electrophoresis ◽

Starch Gel Electrophoresis ◽

Esterase Isozyme ◽

Esterase Isozymes ◽

Isozyme Patterns ◽

Barley Cultivars ◽

Starch Gel

Fifty-five currently licensed Canadian cultivars and some parental genotypes were analyzed by starch-gel electrophoresis for esterase isozyme patterns and extent of polymorphism for these isozymes. Each cultivar was assigned to one of nine different patterns observed. Fifty-one percent (28) of the cultivars exhibited polymorphic isozyme patterns. The polymorphism was a varietal characteristic and apparently not associated with the age of the cultivar or area of adaptability.

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The nature of the multiple forms of cytoplasmic aspartate aminotransferase from pig and sheep heart

Biochemical Journal ◽

10.1042/bj1410401 ◽

1974 ◽

Vol 141 (2) ◽

pp. 401-406 ◽

Cited By ~ 20

Author(s):

Robert John ◽

Richard Jones

Keyword(s):

Aspartate Aminotransferase ◽

Gel Electrophoresis ◽

Starch Gel Electrophoresis ◽

Wide Range ◽

Covalent Structure ◽

Starch Gel ◽

The Difference ◽

Ph Range ◽

The Relationship ◽

Charged Group

Starch-gel electrophoresis of sheep heart aspartate aminotransferase was carried out over the range pH7.0–8.5. The enzyme separates into three subforms in the same way as the pig heart enzyme. As the pH was increased the distance migrated by each subform increased by the same amount, so that they remained the same distance apart. Titration of the enzyme over the appropriate pH range was used to calculate the difference in charge between the subforms and it was concluded that they differ by one charged group per dimer from their nearest neighbour on the electrophoretogram over the whole pH range studied. It was also shown that the pig-heart α and β subforms differ by almost one charged group per dimer in the range pH5.5–5.7 and that the spacing between the subforms on starch-gel electrophoresis at pH8.0 is the same as that for the sheep enzyme. Since the charge difference between the subforms is maintained over such a wide range of pH, it is concluded that they probably differ from each other in covalent structure, because of the improbability that conformational differences can give rise to such behaviour. The relationship between the subforms and inactive binding of the coenzyme is also examined.

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Physicochemical and Biochemical Properties of Commercially Available Urokinase Preparations

10.1055/s-0039-1680457 ◽

1977 ◽

Author(s):

M. Nishida ◽

H. Nishimaki ◽

S. Miyake ◽

T. Suyama ◽

S. Morisue

Keyword(s):

Gel Electrophoresis ◽

Molecular Form ◽

Sodium Dodecyl ◽

Gel Filtration ◽

Biochemical Properties ◽

Molecular Forms ◽

Starch Gel Electrophoresis ◽

Starch Gel ◽

The Difference ◽

Fresh Urine

Comparative studies were made on eleven urokinase preparations commercially available. Analysis by both gel filtration and sodium dodecyl gel electrophoresis revealed the variety of molecular forms of the activator in the preparations showing molecular weight approximately 54,000 (A), 47,000 (B) and 34,000 (C). Starch gel electrophoresis at pH 8.8 indicated that (B) and (C) moved to anode whereas (A) and the active component of fresh urine slightly moved to the cathod. Proteolytic digestion of (A) produced the same component as shown by (B) and (C) on starch gel electrophoresis. Plasminogen activating activity of (B) and (C) was found to be less than that of (A) when measured by the procedure of CTA fibrinolytic method with the physiological blood level of plasminogen. The present data suggest that variety of molecular form in the preparation may be due to the difference of purification procedure in view of proteolytic degradation of the enzyme, and (A) seems to be the naturally occuring type of urokinase in urine.

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ASSOCIATION OF SERUM HEMOPEXIN, TRANSFERRIN, PREALBUMIN AND ALBUMIN1 TYPES WITH PRODUCTIVE TRAITS OF YORKSHIRE AND LACOMBE BREEDS OF PIGS

Canadian Journal of Animal Science ◽

10.4141/cjas69-033 ◽

1969 ◽

Vol 49 (2) ◽

pp. 223-229 ◽

Cited By ~ 2

Author(s):

V. N. Tripathi ◽

W. E. Howell

Keyword(s):

Serum Protein ◽

Gel Electrophoresis ◽

Performance Test ◽

Carcass Characteristics ◽

Correlated Response ◽

Starch Gel Electrophoresis ◽

Starch Gel ◽

The Difference ◽

Productive Traits ◽

Daily Gain

Sera from 354 Yorkshire and 97 Lacombe pigs on official Canadian Record of Performance test were analyzed by starch gel electrophoresis to determine their hemopexin, transferrin, prealbumin and albumin1 types. Estimates of the possible effects of different serum protein types on daily gain on test, age at slaughter adjusted to 70.37 kg carcass weight and seven other carcass characteristics were obtained by least squares methods. Significant associations were observed between each of the four serum protein loci and at least one of the nine productive traits in the Yorkshire breed. In the Lacombe breed only the prealbumin locus, which was associated with total backfat thickness, had any effect on any one of the nine productive traits. Since the results for the two breeds were not in agreement with each other and the magnitude of the difference between extremes was small, it was concluded that a correlated response in swine performance could not be expected from selection on the basis of serum protein polymorphism.

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Bovine Platelet Proteins III. Some Properties of Platelet Fibrinogen

Thrombosis and Haemostasis ◽

10.1055/s-0038-1653557 ◽

1969 ◽

Vol 21 (03) ◽

pp. 428-440 ◽

Cited By ~ 8

Author(s):

N. O Solum ◽

S Łopaciuk

Keyword(s):

Intrinsic Viscosity ◽

Rabbit Antiserum ◽

Disc Electrophoresis ◽

Carbohydrate Content ◽

Plasma Fibrinogen ◽

Total Amino Acid ◽

Electrophoretic Mobilities ◽

Bovine Plasma ◽

Starch Gel ◽

The Difference

Summary1. Some properties of purified bovine platelet fibrinogen have been described and the data compared to those obtained by parallel analysis of purified bovine plasma fibrinogen.2. A close similarity was found between platelet and plasma fibrinogen as to sedimentation coefficients, electrophoretic mobilities in starch gel and polyacrylamide disc electrophoresis, light absorption spectra in the range 240 mμ to 330 mμ, ability to form immunoprecipitate with a rabbit antiserum against bovine plasma fibrinogen, total amino acid composition and in N-terminal amino acids.Differences between the fibrinogens were found as to intrinsic viscosity, carbohydrate content and behaviour upon clotting by thrombin. Intrinsic viscosity in 0.3 M NaCl at 25° was 0.48 dl/g for platelet fibrinogen as compared to 0.26 dl/g for plasma fibrinogen. The carbohydrate content of platelet fibrinogen was 0.56 ± 0.10% 1.56±0.10% and 1.37±0.09% for sialic acid (calculated as N-glycolyl neuraminic acid), hexose (galactose/mannose 1:2) and hexosamine (glucosamine), respectively. These values were 6, 54 and 26% higher than those found for plasma fibrinogen. The difference in clotting behaviour indicated a slower polymerization rate of the fibrin monomers formed from platelet fibrinogen than of those formed from plasma fibrinogen.

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Bovine Platelet Proteins II. Purification of Platelet Fibrinogen

Thrombosis and Haemostasis ◽

10.1055/s-0038-1653556 ◽

1969 ◽

Vol 21 (03) ◽

pp. 419-427 ◽

Cited By ~ 5

Author(s):

N. O Solum ◽

S Łopaciuk

Keyword(s):

Analytical Ultracentrifugation ◽

Insoluble Fraction ◽

Disc Electrophoresis ◽

Plasma Fibrinogen ◽

Starch Gel Electrophoresis ◽

Freezing And Thawing ◽

Insoluble Material ◽

High Resolution Power ◽

Starch Gel ◽

Platelet Proteins

Summary1. Platelet fibrinogen has been purified from washed bovine platelets. The procedure was based on the methods for purification of plasma fibrinogen by fractionated precipitations and extractions with ethanol and glycine below 0°, and precipitation of proteins by dimethylformamide at 0°.2. The platelet extract obtained by freezing and thawing of the cells, freed from insoluble material by centrifugation at 23,000 x g for 30 min, contained 0.22 ±0.003mg fibrinogen per 109 platelets. Total protein of this fraction was 0.77 ±0.08 mg per 109 platelets whereas that of the insoluble fraction was 0.79 ±0.09 mg per 109 platelets.3. The most purified platelet fibrinogen fraction contained 91-98% of the protein in a thrombin-clottable state. The yield was approx. 20%. It showed homogeneity in analytical ultracentrifugation, in immunoelectrophoresis using an antiserum produced by immunization of rabbits against platelet extract, and in starch gel electrophoresis using a discontinuous system of Tris HCl and borate buffers offering a high resolution power towards the platelet proteins. Polyacrylamide disc electrophoresis revealed two to three faint lines behind the main fibrinogen line. At least one such line was also observed with purified plasma fibrinogen.

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Fractionation of Plasminogen by Starch Gel Electrophoresis

Thrombosis and Haemostasis ◽

10.1055/s-0038-1655580 ◽

1964 ◽

Vol 12 (01) ◽

pp. 126-136 ◽

Cited By ~ 2

Author(s):

Karl H. Slotta ◽

J. D Gonzalez

Keyword(s):

Gel Electrophoresis ◽

Room Temperature ◽

Broad Band ◽

Caproic Acid ◽

Starch Gel Electrophoresis ◽

Full Activity ◽

Veronal Buffer ◽

Starch Gel ◽

Alkaline Range

SummaryWhen urea or ε-amino caproic acid were used as solublizing agents for plasminogen in electrophoretic experiments, only one broad band of the proenzyme was obtained on acetate cellulose, in starch block, and in acrylamide gel. In starch gel electrophoresis, however, both forms of plasminogen – the native or euglobulin and Kline’s or Pseudoglobulin plasminogen – separated into six bands. These migrated toward the cathode at room temperature in borate or veronal buffer in the alkaline range and showed full activity in fibrinagar-streptokinase plates.

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PROTEIN POLYMORPHISMS, SEGREGATION IN GENETIC CROSSES AND GENETIC DISTANCES AMONG FISHES OF THE GENUS XIPHOPHORUS (POECILIIDAE)

Genetics ◽

10.1093/genetics/102.3.539 ◽

1982 ◽

Vol 102 (3) ◽

pp. 539-556

Author(s):

Don C Morizot ◽

Michael J Siciliano

Keyword(s):

Goodness Of Fit ◽

Inbred Strains ◽

Interspecific Backcross ◽

Genetic Distances ◽

Rapid Expansion ◽

Starch Gel Electrophoresis ◽

Lower Vertebrate ◽

Protein Coding ◽

Group I ◽

Starch Gel

ABSTRACT The products of 49 protein-coding loci were examined by starch gel electrophoresis for populational variation in six species of Xiphophorus fishes and/or segregation in intra- and interspecific backcross and intercross hybrids. Electrophoretic variation was observed for 29 of the 35 locus products in a survey of 42 population samples. The highest frequency of polymorphic loci observed in noninbred populations was 0.143. After ten or more generations of inbreeding, all loci studied were monomorphic. Inbred strains generally exhibited the commonest electrophoretic alleles of the population from which they were derived. An assessment of genetic distances among Xiphophorus populations reflected classical systematic relationships and suggested incipient subspeciation between X. maculatus from different drainages as well as several species groups. Thirty-three loci were analyzed with respect to segregation in hybrids. The goodness of fit of segregations to Mendelian expectations at all loci analyzed (except loci in linkage group I) is interpreted as evidence for high genetic compatibility of the genomes of Xiphophorus species. It is anticipated that these data will result in a rapid expansion of the assignment of protein-coding loci to linkage groups in these lower vertebrate species.

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