MULTIPLE FORMS OF LACTATE DEHYDROGENASE AND ASPARTATE AMINOTRANSFERASE IN HERRING (CLUPEA HARENGUS HARENGUS L.)

1966 ◽  
Vol 44 (10) ◽  
pp. 1319-1326 ◽  
Author(s):  
Paul H. Odense ◽  
Theresa M. Allen ◽  
Ted C. Leung
Keyword(s):  
Lactate Dehydrogenase ◽  
Binomial Distribution ◽  
Aspartate Aminotransferase ◽  
Frozen Storage ◽  
Electrophoretic Pattern ◽  
Clupea Harengus ◽  
Starch Gel Electrophoresis ◽  
Hybrid Form ◽  
Starch Gel ◽  
Clupea Harengus Harengus

The distribution of isoenzymes of lactate dehydrogenase (LDH) and aspartate aminotransferase (AAT) in the tissues of 189 herring (Clupea harengus harengus L.) were examined. Starch-gel electrophoresis of the LDH isoenzymes of the herring revealed the presence of two hybrid forms representing mutant alleles at the B locus. These mutants gave rise to two genotypes, BB′ and BB″, whose LDH staining patterns revealed a binomial distribution of the tetramer combinations formed from a free and random association of the A, B, and B′, and the A, B, and B″ monomers respectively.A hybrid form of soluble AAT was found. Its electrophoretic pattern showed a 1:2:1 binomial distribution of bands. It is postulated that these bands represent AAT dimers formed from normal S and mutant S′ monomers of a heterozygous SS′ genotype. The normal homozygous SS genotype showed only one band of activity.The normal levels of LDH and AAT activity in plasma and in heart and skeletal muscles were determined. During frozen storage LDH-5 activity gradually disappeared, while LDH-1 activity changed least; LDH-1 was also most stable at higher temperatures. Frozen storage rapidly destroyed AAT activity.

Stock Definition in Atlantic Herring (Clupea harengus harengus): Genetic Evidence for Discrete Fall and Spring Spawning Populations

1982 ◽  
Vol 39 (12) ◽  
pp. 1610-1621 ◽  
Author(s):  
Irv Kornfield ◽  
Bruce D. Sidell ◽  
P. S. Gagnon
Keyword(s):  
Gulf Of Maine ◽  
Temporal Stability ◽  
Clupea Harengus ◽  
Atlantic Herring ◽  
Starch Gel Electrophoresis ◽  
Contingency Analysis ◽  
Gene Frequencies ◽  
Genetic Population ◽  
Starch Gel ◽  
Clupea Harengus Harengus

Ripe Atlantic herring (Clupea harengus harengus) were sampled from seven discrete spawning grounds in the Gulf of Maine and Gulf of St. Lawrence over a period of 3 yr. Genetic polymorphisms were observed at 13 enzyme loci by starch gel electrophoresis. Five highly polymorphic loci were used to assess population structure of herring stocks by contingency analysis of log-likelihood differences in gene frequencies. Significant temporal variation was observed at several localities. Within both spring spawning and fall spawning populations, significant spatial heterogeneity was noted for particular years, but was not temporally stable. By contrast, overall heterogeneity between spring and fall spawning populations was highly significant indicating genetic isolation of spring spawning populations in the Gulf of St. Lawrence from fall spawning aggregates in the Gulf of St. Lawrence and Gulf of Maine. The low levels of genetic heterogeneity and absence of both temporal stability within fall spawning samples and spatial stability among samples is not consistent with the existence of more than a single genetic population of fall spawning herring in the northwest Atlantic.Key words: Clupea harengus harengus, population genetics, biochemical genetic variation, stock differentiation

scholarly journals MALATE DEHYDROGENASE ISOZYMES OF THE CHICK EMBRYO

1965 ◽  
Vol 13 (6) ◽  
pp. 510-514 ◽  
Author(s):  
JAMES L. CONKLIN ◽  
EDWARD J. NEBEL
Keyword(s):  
Lactate Dehydrogenase ◽  
Chick Embryo ◽  
Malate Dehydrogenase ◽  
Molecular Basis ◽  
Specific Pattern ◽  
Starch Gel Electrophoresis ◽  
Organ Specific ◽  
Malate Dehydrogenase Isozymes ◽  
Starch Gel ◽  
Mitochondrial Malate Dehydrogenase

Malate dehydrogenase fractions of the chick embryo were demonstrated after starch gel electrophoresis of homogenates of liver, brain and spleen. A total of seven malate dehydrogenase fractions were observed to occur in the chick embryo in an organ specific pattern. Treatment of the homogenates with urea, sodium chloride-sodium phosphate, and p-chloromercuribenzoate prior to electrophoresis revealed that only three distinct malate dehydrogenase-active proteins were presence. Two of these proteins exhibited properties similar to those previously reported for the supernatant malate dehydrogenase and mitochondrial malate dehydrogenase of other species. Becuase of the differing properties of chick malate and lactate dehydrogenase it is concluded that the molecular basis for malate dehydrogenase isozymes is different from that reported for lactate dehydrogenase isozymes.

scholarly journals The determination of lactate dehydrogenase isoenzymes in normal human muscle and other tissues

1967 ◽  
Vol 105 (2) ◽  
pp. 599-604 ◽  
Author(s):  
A. E. H. Emery
Keyword(s):  
Lactate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Human Muscle ◽  
Starch Gel Electrophoresis ◽  
Fibrous Connective Tissue ◽  
Starch Gel ◽  
Normal Human ◽  
Lactate Dehydrogenase Isoenzymes ◽  
Good Agreement

1. A technique has been developed, based on preferential inhibition by urea, for determining the amounts and proportions of the M and H sub-units of lactate dehydrogenase (referred to as LDH-M and LDH-H respectively) in human tissues, including muscle. 2. There was good agreement between the results obtained with urea inhibition and those obtained with starch-gel electrophoresis. 3. With increasing age there was a significant decrease in the total amount of lactate dehydrogenase and the amount of LDH-M in skeletal muscle. This could not be accounted for by the replacement of functioning muscle tissue by fibrous connective tissue. 4. The proportion of LDH-M was less in certain muscles (e.g. soleus and extra-ocular) than in other muscles (e.g. gastrocnemius and rectus abdominis). 5. The proportions of LDH-M and LDH-H did not differ significantly in different superficial limb muscles and were not significantly affected by either age or sex. 6. Specimens of muscle from 86 different individuals (all Europeans) have been subjected to electrophoresis, but no variants of lactate dehydrogenase isoenzymes have been found.

GENETIC STUDIES OF ISOZYMES IN NEUROSPORA. I. A STUDY OF EIGHT SPECIES

1971 ◽  
Vol 13 (2) ◽  
pp. 298-305 ◽  
Author(s):  
M. Mohan Reddy ◽  
S. F. H. Threlkeld
Keyword(s):  
Acid Phosphatase ◽  
Lactate Dehydrogenase ◽  
Phosphatase Activity ◽  
Gel Electrophoresis ◽  
Acid Phosphatase Activity ◽  
Starch Gel Electrophoresis ◽  
Acid Phosphatases ◽  
Genetic Studies ◽  
Starch Gel

Mycelial extracts of 34 strains representing eight species of the genus Neurospora were subjected to acrylamide and starch gel electrophoresis to detect sites of esterase, lactate dehydrogenase, amylase, peroxidase, and acid phosphatase activity. Nine isozymes of esterases, four isozymes of lactate dehyrogenases, three isozymes of peroxidases, and two isozymes of acid phosphatases were detected on the gels for the species. The application of zymograms as a biochemical means to characterize species is discussed.

scholarly journals Inheritable Differences in the Electrophoretic Pattern of Hemoglobin Revealed in a Local Random-Bred Colony of Albino Rats

Blood ◽  
1970 ◽  
Vol 35 (4) ◽  
pp. 447-450 ◽  
Author(s):  
JOVO V. MARTINOVIC ◽  
DOBRIVOJE V. MARINKOVIC ◽  
DUSAN T. KANAZIR ◽  
PETER N. MARTINOVITCH
Keyword(s):  
Gel Electrophoresis ◽  
Electrophoretic Pattern ◽  
Albino Rats ◽  
Buffer System ◽  
Starch Gel Electrophoresis ◽  
Parental Type ◽  
Starch Gel ◽  
F2 Generation

Abstract In a local colony of random-bred Albino rats, three different patterns of hemoglobin, arbitrarily denoted as patterns I, II and III, were detected by means of starch-gel electrophoresis in a discontinuous buffer system. Mating experiments showed that rats bearing pattern I and pattern III hemoglobin bred true. Crosses of pattern I with pattern III animals yielded only pattern II animals, and when the latter were mated inter se, the resultant F2 generation showed approximately a ratio of 1:2:1 for patterns I, II and III, respectively. When F1 animals from pattern I with pattern III crosses were mated back to animals of either parental type, the resultant ratio was found to be one pattern II: one pattern I or pattern III.

scholarly journals Isozyme Polymorphisms in Carob Cultivars

HortScience ◽  
1992 ◽  
Vol 27 (3) ◽  
pp. 257-258 ◽  
Author(s):  
J. Tous ◽  
C. Olarte ◽  
M.J. Truco ◽  
P. Arús
Keyword(s):  
Aspartate Aminotransferase ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Ceratonia Siliqua ◽  
Leaf Extracts ◽  
Enzyme Systems ◽  
Starch Gel

The variability of isozymes in nine enzyme systems was studied in 25 carob (Ceratonia siliqua L.) cultivars using starch gel electrophoresis of leaf extracts. Five enzymes (phosphoglucomutase, phosphoglucoisomerase, aspartate aminotransferase, shikimic dehydrogenase, and aconitase) were polymorphic, making it possible for the 25 cultivars to be classified into eight phenotype categories.

Studies on enzyme variation in the murine malaria parasites Plasmodium berghei, P. yoelii, P. vinckei and P. chabaudi by starch gel electrophoresis

Parasitology ◽  
1978 ◽  
Vol 76 (3) ◽  
pp. 241-267 ◽  
Author(s):  
Richard Carter
Keyword(s):  
Lactate Dehydrogenase ◽  
Plasmodium Berghei ◽  
Gel Electrophoresis ◽  
Enzyme Polymorphism ◽  
Genetic Constitution ◽  
Starch Gel Electrophoresis ◽  
Malaria Parasites ◽  
Phosphogluconate Dehydrogenase ◽  
Enzyme Variation ◽  
Starch Gel

SummaryElectrophoretic variation of the enzymes glucose phosphate isomerase, 6-phosphogluconate dehydrogenase, lactate dehydrogenase and glutamate dehydrogenase (NADP-dependent) has been studied in the African murine malaria parasites Plasmodium berghei, P. yoelii, P. vinckei and P. chabaudi and their subspecies. Horizontal starch gel electrophoresis was used throughout. The number of isolates examined in each subspecies varied from 1 (P. y. nigeriensis) to 24 (P. c. chabaudi). Extensive enzyme variation was found among isolates of most of the subspecies from which more than two such isolates were available for study. It is clear that the phenomenon of enzyme polymorphism is of common occurrence among malaria parasites. With the exception of P. berghei and P. yoelii, of which all isolates share an identical electrophoretic form of lactate dehydrogenase, no enzyme forms are shared between any of the 4 species of murine plasmodia. By contrast, within each species common enzyme forms are shared among each of the subspecies. The subspecies are, nevertheless, distinguished from each other by the electrophoretic forms of at least one enzyme.The distribution and reassortment of enzyme variation among isolates of a single subspecies is in accordance with the concept of malaria parasites as sexually reproducing organisms. The study of variation among parasites present in individual wild-caught rodent hosts demonstrates that natural malarial infections usually comprise genetically heterogeneous populations of parasites. Nevertheless, the number of genetically distinct types of parasite of any one species present in a single infected host appears to be small. Generally not more than 2 or 3 clones of parasite of distinct genetic constitution are present in a single infected animal.

Study of Mouse Hemoglobin by Starch-Gel Electrophoresis

1964 ◽  
Vol 13 (2) ◽  
pp. 185-189 ◽  
Author(s):  
T. N. Mehrotra ◽  
Giuseppe Cardinali
Keyword(s):  
Gel Electrophoresis ◽  
Adult Animal ◽  
Electrophoretic Pattern ◽  
Inbred Strains ◽  
Single Band ◽  
Starch Gel Electrophoresis ◽  
Inbred Strains Of Mice ◽  
Starch Gel ◽  
Band Type

SummaryThe hemoglobin pattern of 18 inbred strains of mice was studied by starch-gel electrophoresis. In 7 strains (C57BL/10, C57BL/6, C57BR/cd, C57L, C58, SWR, and SEC/1Re) the electrophoretic pattern was found to be of single-band type: in the remaining 11 strains (AKR, DBA/1, DBA/2, CBA, C3H/He, C3HeB/Fe, Fl/1Re, RF, 129, A, and A/He), 6 components were constantly observed when the electrophoretic run was carried out for 20 hours. Hemoglobin from late C57BL/6 fetuses showed an electrophoretic pattern identical to that of the adult animal. Hemoglobin from AKR and DBA/2 late fetuses and newborns showed an electrophoretic pattern similar to that of the adult animal, but the slowest band was more intensely stained as compared with the corresponding band of the adult animal.

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.

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