scholarly journals Bovine a-Lactalbumin C and aS1-, ß- and ?-Caseins of Bali (Banteng) Cattle, Bos (Bihos) Javanicus

1981 ◽  
Vol 34 (2) ◽  
pp. 149 ◽  
Author(s):  
K Bell ◽  
KE Hopper ◽  
HA McKenzie

An electrophoretic examination is made of milk samples taken from eight Bali (banteng) cattle, Bos (Bibos) javanicus, at Beatrice Hills, Northern Territory, Australia. Starch-gel electrophoresis at pH 8� 5 (NaOH-H3B03 buffer) and filter-paper electrophoresis at pH 8� 6 (diethylbarbiturate buffer) indicate that all samples contain a new a-lactalbumin variant, designated a-lactalbumin C. The order of mobility for bovine variants is A > B > C. The C variant differs from the common B variant in having one more amide residue (substitution of Asn for Asp or GIn for Glu).

1960 ◽  
Vol 04 (03) ◽  
pp. 451-461 ◽  
Author(s):  
Werner Straub

SummaryThe starch gel electrophoresis method of Smithies was applied to the separation of a concentrate of serum clotting factors. The original hydrolysed potato starch, though forming a suitable gel, was not able to separate clotting factors. They are well separated by using a self hydrolysed maize starch. Different batches of this starch show different separation properties according to the degree of hydrolysis. The factor with the highest mobility, i.e. factor X, is highly purified, while the other factors are purified to a certain extent. The protein content does not exceed 2—3 mg% in a solution containing 100 U/ml of one factor and factor X is 2300 times purer than in plasma. The recovery is much better than in paper electrophoresis and 5—10 times more material can be separated in one experiment.The possibilities of this separation method are limited by the fact that the separated clotting factors are distributed along a distance of only 5—10 cm.


1968 ◽  
Vol 107 (2) ◽  
pp. 139-150 ◽  
Author(s):  
R. K. Scopes

1. Details of an improved method for starch-gel electrophoresis of water-soluble muscle proteins are given. 2. Methods are described for detecting enzyme activities on the starch gel after electrophoresis, by using pieces of filter paper. 3. Compositions of incubation mixtures suitable for detecting any of the enzymes of glycolysis, and certain other enzymes, are given. 4. A comparison of the various enzymes in extracts of several muscles from one rabbit was made; most differences are quantitative only. 5. A detailed comparison of the mobilities of various enzymes in extracts of muscles from a wide variety of species was made. Each species was found to have a characteristic pattern of proteins on the starch gel, and the mobilities of individual enzymes varied considerably. 6. Potential uses and extensions of the methods are discussed.


1988 ◽  
Vol 39 (3) ◽  
pp. 317 ◽  
Author(s):  
J Salini ◽  
JB Shaklee

Barramundi, L. calcarifer, were collected from seven localities in the Northern Territory, the Daly, Finniss, Mary, Glyde, Roper and McArthur rivers and Blue Mud Bay, and from the Ord River in Western Australia. Barramundi were sampled seven times from the Daly and Finniss rivers over a 14-month period. In total, 46 loci were identified using starch-gel electrophoresis of enzymes and polyacrylamide electrophoresis of muscle proteins. Twelve loci were polymorphic at the P0.99 level. Most loci were in Hardy-Weinberg equilibrium. A contingency Χ2 analysis for homogeneity of alleles over all loci and all localities was highly significant (P < 0.001). Comparisons of data from adjacent pairs of localities revealed that the overall heterogeneity was attributable to heterogeneity among seven of the eight localities; the Daly and Finniss river areas were not significantly different from one another. No evidence of heterogeneity over time was found among the collections from the Daly River area. The considerable amount of heterogeneity observed suggests that each of these seven localities supports a genetically discrete stock of barramundi; this conclusion is consistent with the documented life history of Australian barramundi. The genetic heterogeneity of the stocks should be considered when management policies for L. calcarifer are being formulated.


1964 ◽  
Vol 12 (01) ◽  
pp. 126-136 ◽  
Author(s):  
Karl H. Slotta ◽  
J. D Gonzalez

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.


Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 595-603
Author(s):  
D Borden ◽  
E T Miller ◽  
D L Nanney ◽  
G S Whitt

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.


1963 ◽  
Vol 41 (1) ◽  
pp. 369-387 ◽  
Author(s):  
J. M. Neelin

By varying conditions of starch gel electrophoresis, factors contributing to the resolution of myogen proteins from chicken breast muscle have been studied. Variables examined included composition of the myogen extractant, protein concentration, ionic strength of electrophoretic media, pH of gel media, plane and direction of electrophoresis, and the nature of cations and anions in gel media and bridge solutions. The significance of anions was more closely studied with constant buffer systems, and gradient systems in which bridge electrolyte differed from, and gradually altered, the gel medium. Optimal separation was obtained in gradient systems with 0.10 M sodium chloride bridge solutions, and gel media of sodium cacodylate, pH 6.9, μ 0.010, which resolved 12 cationic zones, and sodium veronal, pH 7.4, μ 0.010, which resolved 10 anionic zones. These buffers in two-dimensional sequence revealed a total of about 24 components in this myogen.


1981 ◽  
Vol 59 (5) ◽  
pp. 771-775 ◽  
Author(s):  
Moira M. Ferguson ◽  
David L. G. Noakes ◽  
Roy G. Danzmann

Examination of 17 presumptive gene loci by starch-gel electrophoresis revealed differential mobilities only at acid phosphatase-1, alcohol dehydrogenase, esterase-1, and phosphoglucomutase between Nocomis biguttatus and N. micropogon. No intraspecific variation was observed for any loci. The genetic identity (I) and genetic distance (D) were 0.874 and 0.134, respectively. The correlation of electrophoretic mobilities and nuptial tubercle pattern in sexually dimorphic males supports the present taxonomic distinction of these species and provides a simple, unambiguous means of identifying any individuals.Stepwise discriminant function analysis of a series of mensural characters was used to compare fish identified as to species by electrophoresis. At best this correctly assigned fish to their respective species in 85.7% of cases, with a probability of misclassification of 0.1335.This study suggests these two are sibling species, based on a comparison of biochemical and morphological differentiation.


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