Lactate dehydrogenase isoenzyme patterns of gynaecological specimens on starch gel electrophoresis

1968 ◽  
Vol 3 (6) ◽  
pp. 545-IN11 ◽  
Author(s):  
M. Ishihara
Keyword(s):  
Lactate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Dehydrogenase Isoenzyme ◽  
Starch Gel ◽  
Isoenzyme Patterns

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 Growth and isoenzyme comparison of five isolates of Venturia inaequalis

2005 ◽  
Vol 71 (2) ◽  
pp. 65-71 ◽  
Author(s):  
E. Roig ◽  
P. Neumann ◽  
J.-P. Simon
Keyword(s):  
Carbonic Anhydrase ◽  
Gel Electrophoresis ◽  
Venturia Inaequalis ◽  
Starch Gel Electrophoresis ◽  
Enzyme Systems ◽  
Race 1 ◽  
Starch Gel ◽  
Specific Proteins ◽  
Race 2 ◽  
Isoenzyme Patterns

Observation of the mycelial aspect of five isolates representing the fîve races of Venturia inaequalis indicates that it is possible to differentiate these isolates by their growth pattern and the isolate of race 3 appears to be the most easily distinguishable. Fifteen enzyme systems and non-specific proteins have been analyzed by polyacrylamide and starch gel electrophoresis. Thirteen of the isoenzymes systems and non-specific proteins showed no variation among the five isolates. Esterases isoenzyme patterns allow separation of the isolates since only one isoenzyme is common to all isolates and two others are shared by isolates of race 1 and 5. One carbonic anhydrase isoenzyme was observed to be specific to the isolate of race 2.

Isoenzyme Studies in the Identification of Transplanted Muscle in the Mouse

1974 ◽  
Vol 46 (4) ◽  
pp. 555-558 ◽  
Author(s):  
J. S. Neerunjun ◽  
V. Dubowitz
Keyword(s):  
Gel Electrophoresis ◽  
Fibre Type ◽  
Tibialis Anterior ◽  
Isoenzyme Pattern ◽  
Starch Gel Electrophoresis ◽  
Good Marker ◽  
Starch Gel ◽  
Donor Muscle ◽  
Isoenzyme Patterns

1. The isoenzyme pattern of phosphohexose isomerase on starch-gel electrophoresis was found to be significantly and consistently different in the muscles of the Swiss white and 129 ReJ mice. This provided a good marker for identifying donor and host muscle. 2. The isoenzyme pattern does not appear to be due to different proportions of type 1 and 2 fibres or to fibre type grouping as is found in denervated/reinnervated muscle. 3. Tibialis anterior muscles from Swiss white mice were transplanted into the legs of 129 ReJ mice and vice versa. Transplantations between mice of the same strain were used as controls. 4. The isoenzyme patterns from transplanted muscles indicate that it is the donor muscle which regenerates when the tissue is transplanted from one animal to another.

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.

Lactate dehydrogenase isoenzymes in foetal and neonatal tissues

Development ◽  
1964 ◽  
Vol 12 (3) ◽  
pp. 501-509
Author(s):  
A. L. Latner ◽  
A. W. Skillen
Keyword(s):  
Lactate Dehydrogenase ◽  
Distribution Patterns ◽  
Molecular Forms ◽  
Starch Gel Electrophoresis ◽  
Stage Of Development ◽  
Starch Gel ◽  
Visual Demonstration ◽  
Species Specific ◽  
Isoenzyme Patterns ◽  
Lactate Dehydrogenase Isoenzymes

The Existence of isoenzymes, one class of the multiple molecular forms of enzymes, is now well recognized. Isoenzyme distribution patterns, particularly those of lactate dehydrogenase (LDH), have been extensively studied and are often tissue and species specific (Markert & Møller, 1959; Wieland, Pfleiderer, Haupt & Wörner, 1959; Plagemann, Gregory & Wróblewski, 1960; Tsao, 1960). Various techniques, such as zone electrophoresis and column chromatography, have been used to separate isoenzymes of lactate dehydrogenase. Using starch-gel electrophoresis combined with visual demonstration of the isoenzyme patterns, we have detected the usual five zones of activity in human tissues (Latner & Skillen, 1961). They are termed LDl, LD2, LD3, LD4 and LD5 where, according to the terminology we use, the latter is the isoenzyme which migrates furthest towards the anode and is most prominent in heart muscle. It has been suggested that the LDH isoenzyme patterns are specific for each tissue at each stage of development (Markert & Møller, 1959).

Isozymes of lactate dehydrogenase (LDH) in skeletal tissues of the embryonic and newly hatched chick

Development ◽  
1974 ◽  
Vol 31 (1) ◽  
pp. 169-181
Author(s):  
Patricia A. Coffin ◽  
Brian K. Hall
Keyword(s):  
Lactate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Hind Limb ◽  
Relative Activity ◽  
Anaerobic Glycolysis ◽  
Starch Gel Electrophoresis ◽  
Membrane Bone ◽  
Starch Gel ◽  
Aerobic And Anaerobic ◽  
Subsequent Replacement

The time of appearance and the relative activity of isozymes of LDH were studied in portions of the skeleton of the embryonic and newly hatched chick by starch-gel electrophoresis. The following tissues were examined for presence or absence of isozymes: mesenchyme of the hind limb as it separated into chondrogenic and myogenic tissue; the development of the cartilaginous model of the tibia and its subsequent replacement by bone; the development of the quadratojugal (a membrane bone) with and without secondary cartilage. LDH1 and LDH2 were present in all tissues from the earliest time at which the tissues could be detected histologically. Thus these isozymes are ubiquitous. They were also the predominant isozymes during the first and second weeks of development of all the tissues and continued to predominate in the quadratojugal after hatching. LDH3, LDH4, LDH5 appeared after the initial differentiation of the tissues, arose at earlier ages in cartilage than in bone, and became the predominant isozymes earlier in cartilage (14 days of incubation) than in bone (20 days of incubation). These patterns of isozymes were related to metabolic activity of the developing tissues, especially to aerobic and anaerobic glycolysis.

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.

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