THE RESOLUTION OF URINARY OR SERUM PROTEINS BY CHROMATOGRAPHY ON DEAE CELLULOSE COLUMNS WITH PARTICULAR REFERENCE TO URINARY PROTEINS AFTER THERMAL BURNS

1961 ◽  
Vol 39 (5) ◽  
pp. 881-899 ◽  
Author(s):  
S. H. Jackson ◽  
A. W. Farmer ◽  
R. J. Slater ◽  
M. S. DeWolfe
Keyword(s):  
Serum Proteins ◽  
Deae Cellulose ◽  
Ion Concentration ◽  
Starch Gel Electrophoresis ◽  
Urinary Proteins ◽  
Hydrogen Ion Concentration ◽  
Severe Burns ◽  
Protein Excretion ◽  
Starch Gel ◽  
Chromatographic Resolution

Serum proteins were separated into the usual electrophoretic fractions by the starch block technique. Each fraction was then examined by DEAE cellulose chromatography and by starch gel electrophoresis. The combination of starch block electrophoresis and DEAE cellulose chromatography was able to distinguish 22 different serum proteins.The application of DEAE cellulose to the chromatographic resolution of urinary proteins is described. The urine was filtered and the protein was concentrated by ultrafiltration. After dialysis, a suitable aliquot was adsorbed on a DEAE cellulose column and eluted by buffers with a progressively increasing hydrogen ion concentration and ionic strength. Some illustrative chromatographs are given.A number of urines from patients with severe burns were examined by this procedure. The increase in protein excretion was found in all sections of the chromatographs with particular increases in the γ globulin and acid mucoprotein zones.

scholarly journals A chromatographic preparation of ox growth hormone

1966 ◽  
Vol 100 (3) ◽  
pp. 593-600 ◽  
Author(s):  
M Wallis ◽  
HBF Dixon
Keyword(s):  
Molecular Weight ◽  
Growth Hormone ◽  
Gel Electrophoresis ◽  
Anterior Pituitary ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Starch Gel Electrophoresis ◽  
Highly Active ◽  
Cross Linkage ◽  
Starch Gel

1. A method is described for the chromatographic preparation of ox growth hormone. It involves chromatography of an extract of anterior pituitary lobes on DEAE-cellulose, followed by rechromatography on a dextran gel of low cross-linkage (Sephadex G-100). 2. The product is highly active in growth-hormone assays, and is obtained in good yield. It was homogeneous by several criteria, but showed some heterogeneity on starch-gel electrophoresis. 3. The molecular weight of the hormone was estimated from its behaviour on gel-filtration columns under various conditions. Evidence that the hormone may dissociate into sub-units under some conditions is presented.

Starch-gel Electrophoresis of Pig Serum Proteins

Nature ◽  
1963 ◽  
Vol 197 (4873) ◽  
pp. 1201-1201 ◽  
Author(s):  
R. K. SCOPES
Keyword(s):  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Pig Serum

Ultrasonic Effects on lsoenzymes

1966 ◽  
Vol 12 (4) ◽  
pp. 181-186 ◽  
Author(s):  
Clyde A Dubbs
Keyword(s):  
Human Serum ◽  
Ultrasonic Treatment ◽  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Serum Cholinesterase ◽  
Starch Gel Electrophoresis ◽  
Selective Activation ◽  
Intracellular Enzymes ◽  
Starch Gel

Abstract Several significant effects of ultrasonic treatment on human serum cholinesterase and aminopeptidase isoenzymes and on other serum proteins have been found by starch gel electrophoresis. The selective activation of one cholinesterase isoenzyme is especially striking. These effects must be considered when ultrasonic treatment is used for the extraction of intracellular enzymes. When the effects are appreciated, ultrasonics should provide a valuable tool for isoenzyme research.

scholarly journals "Myeloma Protein" in a Patient with Monocytic Leukemia

Blood ◽  
1969 ◽  
Vol 33 (5) ◽  
pp. 746-758 ◽  
Author(s):  
M. DAVE POULIK ◽  
LAWRENCE BERMAN ◽  
ANANDA S. PRASAD
Keyword(s):  
Gamma Globulin ◽  
Plasma Cells ◽  
Serum Proteins ◽  
Protein Profile ◽  
Starch Gel Electrophoresis ◽  
Monocytic Leukemia ◽  
Myeloma Protein ◽  
X Ray ◽  
Starch Gel

Abstract A 74 year old man with monocytic leukemia was found to have serum and urinary protein findings typical of myelomatosis. Lysozyme excretion in the urine was in the range characteristic of monocytic leukemia. There were no x-ray findings indicative of myeloma. Aspirated bone marrow specimens contained one to three per cent plasma cells, and less than 0.1 per cent atypical plasma cells. The leukemia responded temporarily but without remission to treatment with 6MP and steroid, with no effect on the myeloma protein profile or excretion of the urinary proteins. The leukemia was present without overt morphologic or x-ray findings of myeloma, and the case differs from a similar example of the association of myeloma protein with monocytic leukemia in which the leukemia occurred as a terminal event in a previously well-documented myelomatosis. The serum contained a fast-moving "myeloma gamma globulin" which was classified as γ-1, Kappa; Gm. (a + b - f -) Inv. (a). This protein was heterogeneous by starch gel electrophoresis. The urine contained large amounts of lysozyme, Fab, Fc and F'c fragments of the "myeloma gamma globulin," light chains of type Kappa, as well as whole gamma globulin. Small amounts of other serum proteins were also found. The possibility of two neoplastic proliferations involving both the monocytes and plasma cells has been considered. Possible role of monocytoid stem cells with giant nucleoli in the synthesis of "myeloma protein" has been discussed.

STUDIES ON PLASMINOGEN: IV. ALTERATION OF BOVINE AND HUMAN PLASMINOGENS DURING ISOLATION

1966 ◽  
Vol 44 (4) ◽  
pp. 469-473 ◽  
Author(s):  
John Y. S. Chan ◽  
Edwin T. Mertz
Keyword(s):  
Ionic Strength ◽  
Gel Electrophoresis ◽  
Deae Cellulose ◽  
Starch Gel Electrophoresis ◽  
Major Band ◽  
Starch Gel ◽  
Human Plasminogen

Bovine and human plasminogen preparations were analyzed by starch-gel electrophoresis at pH 2.5 and 0.10 ionic strength. The bands were activated with urokinase and the proteolytic and esterolytic activities measured. Bovine euglobulin contains one plasminogen band, B-1. Plasminogen prepared from bovine euglobulin by continuous electrophoresis at pH 3.5 contains B-1 and a faster plasminogen band, B-2. B-1 and B-2 are also found in bovine plasminogen prepared by DEAE-cellulose chromatography. All three preparations on activation give the same two plasmin bands on starch gel. Human euglobulin also contains two active plasminogen bands H-1 and H-2. Plasminogen prepared from human euglobulin by continuous electrophoresis at pH 3.5 contains H-1, H-2, and a faster minor plasminogen band, H-3. All highly purified human plasminogens derived from Cohn fraction III contain either H-3 as a major band and an additional plasminogen band, H-4, or only H-3, but no H-1 and H-2. On activation with urokinase or streptokinase, human plasminogen preparations give one or two plasmin bands. It is concluded that bovine B-2 and human H-3 and H-4 are altered forms of euglobulin plasminogen created during isolation procedures. Essentially pure human H-3 can be prepared by continuous electrophoresis from Cutter plasminogen.

Benzylamine oxidase and histaminase: purification and crystallization of an enzyme from pig plasma

1964 ◽  
Vol 161 (983) ◽  
pp. 153-167 ◽  
Keyword(s):  
Ammonium Sulphate ◽  
Gel Electrophoresis ◽  
Copper Content ◽  
Deae Cellulose ◽  
Starch Gel Electrophoresis ◽  
Anaerobic Conditions ◽  
Concentrated Solutions ◽  
Radioactivation Analysis ◽  
Starch Gel ◽  
Benzylamine Oxidase

The enzyme benzylamine oxidase of pig plasma has been purified and some of the properties of the pure preparation have been studied. The purification procedure included several precipitations with ammonium sulphate and separations of proteins by column chromatography, first on DEAE-cellulose, followed by DEAE-Sephadex and lastly on a hydroxyapatite column. Crystals were prepared from solutions of the purified enzyme by adding ammonium sulphate. The crystalline preparation was homogeneous when studied by starch-gel electrophoresis and by ultracentrifugation. The molecular weight, as determined on the analytical ultracentrifuge, was 195 000. The copper content of the enzyme, as determined by radioactivation analysis, was about four atoms of Cu per molecule of enzyme. Concentrated solutions of the enzyme had a pink colour; the colour disappeared when substrate (benzylamine) was added under anaerobic conditions. The amines which were tested and found to be oxidized by the pure enzyme were: benzylamine, histamine, mescaline and 4-picolylamine. The affinity of the enzyme for benzylamine was more than one hundred times that for histamine.

Nature of Proteinuria Induced by Uranium in Rats

1958 ◽  
Vol 195 (2) ◽  
pp. 354-356 ◽  
Author(s):  
Marguerite Magee ◽  
Harry Foreman
Keyword(s):  
Serum Proteins ◽  
Electrophoretic Pattern ◽  
Urinary Proteins ◽  
Acute Dose ◽  
Protein Excretion ◽  
Filtration Apparatus

Following administration of uranium parenterally into rats in an acute dose, the increase in protein excretion consisted not only of an increase in the normally occurring albumin but to a greater extent an increase in the various globulins. At the height of proteinuria, the electrophoretic pattern of the excreted proteins strongly resembled the pattern of the serum proteins. The appearance of these serum-like urinary proteins suggests a defect in the glomerulus filtration apparatus and provides further evidence that the glomerulus, as well as the tubule, is altered by uranium administration.

scholarly journals THE MECHANISM OF COMPLEMENT ACTION

1920 ◽  
Vol 3 (2) ◽  
pp. 185-201
Author(s):  
S. C. Brooks
Keyword(s):  
Surface Tension ◽  
Serum Proteins ◽  
Ultra Violet ◽  
Hydrogen Ion ◽  
Ion Concentration ◽  
Hydrogen Ion Concentration ◽  
Ion Concentrations ◽  
Ultra Violet Light ◽  
Violet Light ◽  
Molecular Group

It has been shown: 1. That complement exposed to ultra-violet light is not thereby sensitized to the action of heat (which indicates that it is not protein). 2. That inactivation of complement by ultra-violet light is accompanied by a decrease in its surface tension. 3. That photoinactivation of complement is not a result of any changes in hydrogen ion concentration since these are less than 0.05 pH. 4. That hydrogen ion concentrations high enough to transform serum proteins from the cation to the anion condition (i.e. past the isoelectric point) permanently inactivate complement. These facts together with those given in previous papers lead to the following hypotheses. 1. That there is present in serum a hemolytic substance which is formed from a precursor (which may resemble lecithin) and is constantly being formed and simultaneously being broken down into inactive products. 2. That both precursor and lysin contain the same photosensitive molecular group. 3. That the lytic substance is dependent for its activity upon the state of the serum proteins.

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