INHERITED VARIANTS OF α1-ANTITRYPSIN: A NEW ALLELE PiN

1974 ◽  
Vol 16 (2) ◽  
pp. 297-303 ◽  
Author(s):  
Diane Wilson Cox ◽  
Lynne Celhoffer

A new inherited variant of α1-antitrypsin (protease inhibitor or Pi) has been found in five individuals of a family of Welsh origin. The new allele is called PiN, as the α1AT product migrates in acid starch gel between the products of the PiM and PiP alleles. The individuals carrying the PiN allele are all of Pi type MN. The new variant has been compared in several electrophoretic systems with other variants migrating in a similar region by acid starch gel electrophoresis (M, P, S, V, W and X). Acid starch gel and crossed antigen-antibody electrophoresis are most suitable for distinguishing the PiN product. By immunofixation electrophoresis, N has a mobility only slightly different from that of M, however the value of this method can be seen for distinguishing other slow variants which cannot be clearly distinguished on acid starch gels. Twenty-three variants of α1AT are now known. Twenty-two of these are electrophoretic variants and one, the null allele (Pi−), produces no α1AT.

1970 ◽  
Vol 27 (5) ◽  
pp. 943-945 ◽  
Author(s):  
A. G. Johnson ◽  
F. M. Utter ◽  
H. O. Hodgins

Three phenotypes of L-alpha-glycerophosphate dehydrogenase (α-GPDH) were found in muscle extracts of Pacific ocean perch by starch-gel electrophoresis. No association was obvious between alpha-glycerophosphate phenotype and sex or stage of maturity. The observed phenotypes were presumed to be under the control of two allelic genes, F and S. This assumption was supported by the distribution of phenotypes of fish collected off the coasts of Washington and Oregon. This report is the first on genetic variants of an enzyme in Pacific ocean perch and suggests that isozymes of α-GPDH may be useful in population studies of this species.


1988 ◽  
Vol 79 (5) ◽  
pp. 359-365 ◽  
Author(s):  
D. C. Brown ◽  
I. J. Ropson ◽  
D. A. Powers

Abstract Starch gel electrophoresis has shown that natural populations of Fundulus heteroclitus have electrophoretic variants for at least 21 loci. We provide inheritance data for 10 polymorphic systems: esterases (Est-B, EST-C, and Est-D); aspartate amlnotransferases (Aat-A, and Aat-B); mannosephosphate isomerase (Mpl-A); acid phosphatase (Ap-A); phosphoglucomutase (Pgm-B); hexose-6-phosphate dehydrogenase (H6pdh-A); and fumarase (Fum-A). Variants for nine of these loci segregate as autosomally inherited codominant alleles. The other system, EST-C, does not reflect such inheritance. We have identified two possible linkage groups: H6pdh-A may be loosely linked to Pgm-B, and Fum-A appears to be linked to Pgm-A. Tissue specificity and intracellular localization for all these loci are also presented.


1967 ◽  
Vol 45 (2) ◽  
pp. 221-237 ◽  
Author(s):  
W. W. Dillon ◽  
R. G. Romans

Chromatography of insulin, on carboxymethyl (CM) cellulose columns in urea-containing buffers, revealed the presence of at least five components, one major and four minor, in commercial insulin. This fractionation is related to other chromatographic fractionations of insulin and the nature of the minor components is discussed.Insulin which had been incubated in HCl was chromatographed. The behavior of the incubated products on the column showed that two or more amide groups were hydrolyzed simultaneously but at different rates. Because of the anomalous behavior of one of the components, it is postulated that a group other than the amides is also transformed during acid incubation. This component is present in commercial insulin samples.The electrophoretic separation of insulin in urea–starch gels was shown to be due to charge differences on the molecules rather than size differences. Correlation of the components separated on the CM-cellulose column with those separated in the urea–starch gel electrophoresis showed that much smaller charge differences on the molecules are distinguished on the CM-cellulose column than in the gel.


1968 ◽  
Vol 10 (4) ◽  
pp. 961-967 ◽  
Author(s):  
A. A. Grunder

Three regions of serum esterase activity of chickens were differentiated by means of starch gel electrophoresis and appropriate stains. Regions I and II seemed to represent aliesterase while region III apparently represented a cholinesterase. The patterns of zones of region I were classified into three phenotypes named A, B, and AB and the hypothesis was proposed that these are controlled by two codominant alleles named EsA and AsB. The staining intensity of these esterase zones among adults was sex-associated in that the mean staining intensity of zones was greater in male than in female sera. Frequency of the EsB allele was 0.70, 0.76, and 0.85 in three meat lines.


1975 ◽  
Vol 42 (2) ◽  
pp. 277-283 ◽  
Author(s):  
H. S. Juffs

SummaryStarch-gel electrophoresis (SGE) and formol titration methods for detecting proteolysis in cold-stored raw milk have been studied to establish their value as quality indices. When examined by SGE, the first evidence of proteolysis in raw milks stored at 5°C was the formation of para-κ-casein. However, this fraction could not be detected on the starch gels until the total bacterial count (TBC) exceeded 107/ml. The SGE method appeared more reliable than the previously discussed tyrosine value method. Formol titration did not appear to have any application in the screening of cold-stored raw milks with TBC < 107/ml, but would detect some milks of poorer bacteriological quality.


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.


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