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.

Amine-Citrate Buffers for pH Control in Starch Gel Electrophoresis

1972 ◽  
Vol 29 (8) ◽  
pp. 1169-1172 ◽  
Author(s):  
J. W. Clayton ◽  
D. N. Tretiak
Keyword(s):  
Gel Electrophoresis ◽  
Ph Control ◽  
Starch Gel Electrophoresis ◽  
Good Resolution ◽  
Citrate Buffer ◽  
Starch Gel ◽  
Ph Range ◽  
Amine Buffers

Amine-citrate buffer systems for pH control in starch gel electrophoresis gave good resolution of some dehydrogenase isozymes. The pK's of three new amine buffers, N-(3-aminopropyl)-morpholine, pK2 25 C, 6.12; N-(3-aminopropyl)-diethanolamine, pK2 25 C, 6.90; and 1,3-bis(dimethylamino)-2-propanol, pK2 25 C, 7.55, were determined at 5 C intervals in the range 10–40 C. These compounds, together with N, N-bis(2-hydroxyethyl)iminotris(hydroxymethyl)methane (bis-Tris) and tris-(hydroxymethyl)-methylamine(Tris), provide a series of amine buffers with pK's at 0.5 unit intervals in the pH range 6.1–8.1.

The relationship between nematodes of the genus Cosmocercoides Wilkie, 1930 (Nematoda: Cosmocercoidea) in toads (Bufo americanus) and slugs (Deroceras laeve)

1987 ◽  
Vol 65 (7) ◽  
pp. 1650-1661 ◽  
Author(s):  
Daryl J. Vanderburgh ◽  
R. C. Anderson
Keyword(s):  
Discriminant Analysis ◽  
Gel Electrophoresis ◽  
Analysis Of Covariance ◽  
Starch Gel Electrophoresis ◽  
Bufo Americanus ◽  
Cross Transmission ◽  
Starch Gel ◽  
The Relationship

Nematodes of the genus Cosmocercoides Wilkie, 1930 from Bufo americanus and Deroceras laeve, generally considered to belong to the same species (Cosmocercoides dukae), were compared. Male worms from B. americanus had 20 or 21 rosette papillae per subventral row whereas males from D. laeve had 13 to 14. Worms from toads had numerous simple postanal papillae. Worms from slugs generally lacked such papillae. Worms from the two hosts differed morphometrically and were well separated by discriminant analysis after bias of worm length was removed by analysis of covariance. Differences in isoenzyme migration were detected using starch gel electrophoresis. In cross-transmission experiments, more toads became infected when exposed to larvae of worms from toads than when exposed to larvae of worms from slugs. More slugs became infected when exposed to larvae from slugs than when exposed to larvae from toads. Intensity of mature worms recovered was significantly (p < 0.05) greater (and patent infections developed) when transmission was from toad to toad or from slug to slug than when transmission was from toad to slug or from slug to toad. No patent infections were recorded from toads or slugs exposed to larvae from the unrelated host. The results indicate that worms in toads and slugs are not conspecific. Cosmocercoides variabilis (Harwood, 1930) Travassos, 1931 is resurrected as the name of the species occurring in B. americanus, Cosmoceroides dukae (Holl, 1928) Travassos, 1931 is retained as the name of the species occurring in D. laeve.

scholarly journals The relationship between reversibility of fibril formation and subunit composition of rat skin collagen

1969 ◽  
Vol 113 (2) ◽  
pp. 419-422 ◽  
Author(s):  
D. W. Bannister
Keyword(s):  
Acetic Acid ◽  
Gel Electrophoresis ◽  
Fibril Formation ◽  
Subunit Composition ◽  
Starch Gel Electrophoresis ◽  
Rat Skin ◽  
Fractionation Procedure ◽  
Skin Collagen ◽  
Starch Gel ◽  
The Relationship

1. Salt-soluble rat skin collagen was precipitated from solution at neutral pH and 37°. On cooling, a portion of the collagen returned into solution. The fractions were separated, the supernatant was concentrated and the precipitate was redissolved in dilute acetic acid. 2. Solutions of supernatant and precipitate were subjected to the same fractionation procedure, giving four fractions. 3. Each fraction was examined by starch-gel electrophoresis and a relationship between subunit composition and the fractionation procedure was noted. The collagen that redissolved on cooling contained less of the more highly cross-linked components than did either the fraction remaining in the precipitate or the starting material.

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.

scholarly journals Lactic Dehydrogenase of Human Chronic Lymphocytic Leukemic Leukocytes

Blood ◽  
1966 ◽  
Vol 27 (1) ◽  
pp. 85-92 ◽  
Author(s):  
RICHARD H. BOTTOMLEY ◽  
S. J. LOCKE ◽  
H. C. INGRAM
Keyword(s):  
Gel Electrophoresis ◽  
Migration Rate ◽  
Lactic Dehydrogenase ◽  
Isozyme Pattern ◽  
Lymphocytic Leukemia ◽  
Starch Gel Electrophoresis ◽  
Ldh Activity ◽  
Isozyme Band ◽  
Wide Range ◽  
Starch Gel

Abstract Lactic dehydrogenase was quantitated and its isozyme pattern studied in the leukocytes of 10 patients with chronic lymphocytic leukemia. There was a wide range of LDH activity, although all isozyme patterns by starch-gel electrophoresis showed greatest activity in the No. III isozyme band. Comparison of the rate of migration of the leukemic leukocyte LDH with LDH from normal leukocytes and erythrocytes showed no difference in migration rate, suggesting that the LDH of chronic lymphocytic leukemic leukocytes does not differ in electrical charge from LDH of normal leukocytes.

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.

scholarly journals PHYSICOCHEMICAL CHARACTERIZATION OF MOUSE MYELOMA PROTEINS: DEMONSTRATION OF HETEROGENEITY FOR EACH MYELOMA GLOBULIN

1961 ◽  
Vol 114 (3) ◽  
pp. 399-413 ◽  
Author(s):  
John L. Fahey
Keyword(s):  
Gel Electrophoresis ◽  
Physicochemical Characterization ◽  
Physicochemical Characteristics ◽  
Starch Gel Electrophoresis ◽  
Myeloma Protein ◽  
Myeloma Proteins ◽  
Wide Range ◽  
Starch Gel ◽  
Mouse Myeloma

Physicochemical characterization of mouse myeloma proteins revealed the individuality of each myeloma protein. When the myeloma proteins are considered collectively a wide range of individual properties were represented, including electrophoretic mobilities varying from the gamma to alpha region, hexose contents from 1 to 4 per cent, and ultracentrifugal components from 6.5 to 13 S. The 20 myeloma proteins could be divided into groups, the gamma type and the beta type myeloma globulins, on the basis of physicochemical, as well as immunoelectrophoretic, studies. Two gamma type myeloma proteins (5563, MPC-11) resembled normal gamma globulins, sedimenting as a single 6.5 S peak in the ultracentrifuge, and having a relatively low hexose content (1 per cent). Eighteen beta type mouse myeloma proteins differed from gamma myeloma proteins and, typically, were found on ultracentrifugal analysis to have multiple components with sedimentation coefficients of 6.5, 9, 11, and 13 S, having a higher hexose content (2 to 4 per cent) as well as distinctive chromatographic and starch gel electrophoretic properties. All of the mouse myeloma proteins were heterogeneous and heterogeneity of two types was observed. Polymer formation was responsible for the 9, 11, and/or 13 S components seen on ultracentrifugation of the beta type myeloma proteins. Starch gel electrophoresis revealed this type of heterogeneity as relatively widely separated myeloma protein components, presumably owing to the retardation effect of starch gel on the electrophoretic migration of the larger polymers. Starch gel electrophoresis revealed a different type of heterogeneity for the two gamma type myeloma proteins, each of these being shown to contain 5 or more components differing only in electrophoretic properties. The physicochemical characteristics of the γ-type and ß-type myeloma proteins in the mouse indicated the close similarity of these proteins to the γ- and ß-2A-myeloma proteins in man.

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.

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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