scholarly journals Effect of alloxan-diabetes on multiple forms of hexokinase in adipose tissue and lung

1967 ◽  
Vol 105 (3) ◽  
pp. 1301-1305 ◽  
Author(s):  
Patricia McLean ◽  
J. Brown ◽  
Eileen Walters ◽  
K. Greenslade
Keyword(s):  
Adipose Tissue ◽  
Gel Electrophoresis ◽  
Alloxan Diabetes ◽  
Diabetic Rats ◽  
Type I ◽  
Starch Gel Electrophoresis ◽  
Type Ii ◽  
Multiple Forms ◽  
Starch Gel ◽  
Hexokinase Type I

Comparison has been made of the effect of alloxan-diabetes on the multiple forms of hexokinase (EC 2.7.1.1) in adipose tissue and lung. Types I and II hexokinase were distinguished in adipose tissue by their different stabilities to heat treatment, which made it possible to determine the activity of each form spectrophotometrically; additional confirmatory evidence was obtained from starch-gel electrophoresis. Type II hexokinase was markedly depressed in adipose tissue from alloxan-diabetic rats. Lung contained types I, II and III hexokinase, type I predominating. There was no significant change in the pattern of these multiple forms of hexokinase in lung from alloxan-diabetic rats. These results are discussed in relation to current ideas that the insulin-sensitivity of a tissue may be correlated with the content of type II hexokinase.

scholarly journals The distribution of some hydrolases in glomeruli and tubular fragments prepared from rat kidney by zonal centrifugation

1971 ◽  
Vol 122 (5) ◽  
pp. 641-645 ◽  
Author(s):  
D. G. Taylor ◽  
R. G. Price ◽  
D. Robinson
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Gel Electrophoresis ◽  
Leucine Aminopeptidase ◽  
Rat Kidney ◽  
Kidney Cortex ◽  
Starch Gel Electrophoresis ◽  
Multiple Forms ◽  
Rat Kidney Cortex ◽  
Starch Gel

1. A collagenase digest of rat kidney cortex was separated into four bands by zonal centrifugation. 2. Two of these bands were shown by light-microscopy to contain glomeruli and tubular fragments, which were free from each other and well separated from other renal material. 3. Protein, N-acetyl-β-glucosaminidase, 5′-nucleotidase, l-leucine β-naphthylamidase, leucine aminopeptidase, acid phosphatase and alkaline phosphatase were assayed across the gradient. 4. The greater proportion of these enzyme activities was recovered in the tubular fragments and acid phosphatase was the only enzyme detected in significant amounts in the glomeruli. 5. Tubular fragments and glomeruli were sedimented and multiple forms of β-naphthylamidase, N-acetyl-β-glucosaminidase, acid phosphatase and alkaline phosphatase were investigated by starch-gel electrophoresis.

Detection of multiple forms of proteolytic enzymes by starch gel electrophoresis

1968 ◽  
Vol 46 (10) ◽  
pp. 1317-1320 ◽  
Author(s):  
E. kaminski ◽  
W. Bushuk
Keyword(s):  
Ionic Strength ◽  
Gel Electrophoresis ◽  
Direct Detection ◽  
Proteolytic Enzymes ◽  
Urea Concentration ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Separation ◽  
Multiple Forms ◽  
Starch Gel ◽  
Sensitive Method

A rapid and sensitive method for the direct detection of multiple forms of proteolytic enzymes by starch gel electrophoresis is described. The location of the enzyme components is identified by the degradation of hemoglobin which is included in the starch gel. This method was used to identify the enzyme components of the 10 commercial proteolytic enzymes bromelain, chymotrypsin, ficin, papain, pepsin, pronase B, protease, proteinase, and two preparations of trypsin. The effects of urea concentration and the ionic strength of aluminium lactate buffer were also examined. The best results were obtained with 3 M urea and with an ionic strength of 0.1 for the lactate buffer. It was observed that the number of enzyme components decreased with increasing concentrations of urea or increasing ionic strength of lactate buffer. The number of enzyme components did not always correspond to the number of protein bands. Self-digestion occurred in some of the protein bands in the starch gel after electrophoretic separation of the proteolytic enzymes.

scholarly journals The effect of anti-insulin serum and alloxan-diabetes on the distribution and multiple forms of hexokinase in lactating rat mammary gland

1968 ◽  
Vol 109 (5) ◽  
pp. 737-741 ◽  
Author(s):  
Eileen Walters ◽  
Patricia McLean
Keyword(s):  
Mammary Gland ◽  
Soluble Fraction ◽  
Diabetic Rats ◽  
Particulate Fraction ◽  
Type I ◽  
Type Ii ◽  
Multiple Forms ◽  
Hexokinase Activity ◽  
Control Value ◽  
Rat Mammary Gland

1. The distribution and multiple forms of hexokinase activity in lactating rat mammary gland were investigated in alloxan-diabetic rats and in rats treated with anti-insulin serum. It was found that 46% of the total hexokinase of mammary-gland tissue from control rats was in the particulate fraction, but this percentage was decreased in the alloxan-diabetic rats to 11% of the total hexokinase. The hexokinase activity of the soluble fraction was not significantly altered but there was a decrease in the type II/type I quotient. 2. The early changes that occurred on insulin deprivation were studied 1hr. after administration of anti-insulin serum to lactating rats, at which time the hexokinase bound to the particulate fraction had decreased to 11% of the control value and that in the soluble fraction had increased by approx. 50%. The hexokinase type II/type I quotient in the soluble fraction was significantly decreased. These results suggested that there was a release of particulate-bound hexokinase in rats treated with anti-insulin serum.

scholarly journals ANTIGENIC RELATIONSHIPS OF BENCE JONES PROTEINS, MYELOMA GLOBULINS, AND NORMAL HUMAN γ-GLOBULIN

1963 ◽  
Vol 117 (1) ◽  
pp. 81-104 ◽  
Author(s):  
Shunsuke Migita ◽  
Frank W. Putnam
Keyword(s):  
Type A ◽  
Antigenic Determinants ◽  
Type I ◽  
Starch Gel Electrophoresis ◽  
Type Ii ◽  
Type B ◽  
Bence Jones Protein ◽  
Starch Gel ◽  
Antigenic Relationships ◽  
Bence Jones Proteins

By means of immunodiffusion and immunoelectrophoresis study has been made of antigenic relationships of Bence Jones proteins, and the three classes of normal and pathological immunoglobulins, 7S γ, ß2A, and ß2M. All thirty-nine Bence Jones proteins studied could be classified into either one of two distinct antigenic types, A or B. Both types are related to the immunoelectrophoretically slow (S) fragment of a papain digest of normal γ-globulin; B is related more closely than A, but neither has antigenic determinants in common with the fast (F) fragment. The 7S γ myeloma globulins were either immunological type I or II. The papain digests of these proteins produced the S and F precipitin lines in immunoelectrophoresis but multiple bands in starch gel electrophoresis, especially in the F region. The S fraction of type I myeloma globulins is antigenically similar to Bence Jones protein of type B, and the S component of type II myeloma globulins has antigenic determinants in common with type A Bence Jones protein. Correspondingly, myeloma patients with type I globulins and proteinuria usually excrete type B Bence Jones proteins, whereas patients with type II excrete type A proteins. The F fragment is the part common to normal 7S γ-globulin and types I and II myeloma globulins but is absent in ß2A and ß2M pathological globulins and in both types of Bence Jones proteins. Papain digests of ß2A myeloma globulins produced a single precipitin line in immunoelectrophoresis. ß2A myeloma globulins appeared to have two antigenic units, one in common with type B Bence Jones protein and normal γ-globulin, and another specific to ß2A. The ß2A myeloma patients excreted type B Bence Jones protein. The papain digest of a macroglobulin produced two precipitin lines, the faster of which had antigenic determinants in common with type B Bence Jones protein, the slower seemed specific for the macroglobulin. Five serum micromolecular globulins proved to be either type A or B Bence Jones proteins. From the above results, an antigenic map was constructed showing which determinants are shared and which are specific for normal 7S γ-globulin, types I and II myeloma globulins, ß2A myeloma globulins, a macroglobulin, and types A and B Bence Jones proteins.

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.

scholarly journals THE INHERITANCE OF ENZYME VARIANTS FOR TYROSINE AMINOTRANSFERASE, NADP-DEPENDENT MALATE DEHYDROGENASE, NADP-DEPENDENT ISOCITRATE DEHYDROGENASE, AND TETRAZOLIUM OXIDASE IN TETRAHYMENA PYRIFORMIS, SYNGEN 1

Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 595-603
Author(s):  
D Borden ◽  
E T Miller ◽  
D L Nanney ◽  
G S Whitt
Keyword(s):  
Detailed Analysis ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Tetrahymena Pyriformis ◽  
Tyrosine Aminotransferase ◽  
Breeding Program ◽  
Starch Gel Electrophoresis ◽  
Enzyme Locus ◽  
Starch Gel

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.

STARCH GEL ELECTROPHORESIS OF MYOGEN FROM CHICKEN BREAST MUSCLE IN CONSTANT AND GRADIENT BUFFER SYSTEMS

1963 ◽  
Vol 41 (1) ◽  
pp. 369-387 ◽  
Author(s):  
J. M. Neelin
Keyword(s):  
Gel Electrophoresis ◽  
Protein Concentration ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Starch Gel Electrophoresis ◽  
Two Dimensional ◽  
Sodium Cacodylate ◽  
Gradient Systems ◽  
Optimal Separation ◽  
Starch Gel

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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