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

1969 ◽  
Vol 49 (2) ◽  
pp. 223-229 ◽  
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.

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

1974 ◽  
Vol 141 (2) ◽  
pp. 401-406 ◽  
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.

RELATIONSHIP BETWEEN TRANSFERRIN TYPE AND FEEDLOT PERFORMANCE IN BEEF HEIFERS

1966 ◽  
Vol 46 (3) ◽  
pp. 177-180 ◽  
Author(s):  
M. Makarechian ◽  
W. E. Howell
Keyword(s):  
Least Squares ◽  
Significant Influence ◽  
Gel Electrophoresis ◽  
Carcass Characteristics ◽  
Starch Gel Electrophoresis ◽  
Beef Heifers ◽  
Gene Frequencies ◽  
Feedlot Performance ◽  
Breed Group ◽  
Starch Gel

Sera from 120 feedlot heifers were analyzed by starch gel electrophoresis to determine their transferrin types. Estimates of the possible effects of different transferrin types on gain in the feedlot and some carcass characteristics were obtained by least squares methods. Analysis of variance showed that transferrin type did not have a significant influence on gain and carcass characteristics. Gene frequencies of the different transferrin alleles, derived from a breed group of 79 Hereford heifers, arc also reported.

scholarly journals Physicochemical and Biochemical Properties of Commercially Available Urokinase Preparations

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.

Fractionation of Plasminogen by Starch Gel Electrophoresis

1964 ◽  
Vol 12 (01) ◽  
pp. 126-136 ◽  
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.

scholarly journals THE INHERITANCE OF ENZYME VARIANTS FOR TYROSINE AMINOTRANSFERASE, NADP-DEPENDENT MALATE DEHYDROGENASE, NADP-DEPENDENT ISOCITRATE DEHYDROGENASE, AND TETRAZOLIUM OXIDASE IN TETRAHYMENA PYRIFORMIS, SYNGEN 1

Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 595-603
Author(s):  
D Borden ◽  
E T Miller ◽  
D L Nanney ◽  
G S Whitt
Keyword(s):  
Detailed Analysis ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Tetrahymena Pyriformis ◽  
Tyrosine Aminotransferase ◽  
Breeding Program ◽  
Starch Gel Electrophoresis ◽  
Enzyme Locus ◽  
Starch Gel

ABSTRACT The isozymic patterns of tyrosine aminotransferase, NADP malate dehydrogenase, NADP isocitrate dehydrogenase, and tetrazolium oxidase were examined by starch-gel electrophoresis in Tetrahymena pyriformis, syngen 1. The genetics of the alleles controlling these enzymes was studied through a breeding program. Each enzyme locus was shown to assort vegetatively, as do other loci in this organism. A detailed analysis of the assortment process for the tyrosine aminotransferase locus indicated that the rate of stabilization of heterozygotes into pure types was essentially identical to previously-reported rates for other loci.

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