نتایج جستجو برای: sephadex chromatography
تعداد نتایج: 108287 فیلتر نتایج به سال:
Two tripeptide amides with stuctures similar to thyrotropin releasing hormone were isolated from human seminal fluid and their amino acid sequences determined. The peptides were purified by gel exclusion from Sephadex G50 and were detected by radioimmunoassay with thyrotropin releasing hormone antibody; in addition, N-terminally extended forms were demonstrated by radioimmunoassay after trypsin...
Arylsulfatase A (cerebroside sulfate sulfohydrolase) was purified 3500-fold at a 7% yield from human urine. A crude urinary protein concentrate was prepared by treating pooled urine with ammonium sulfate and subsequently drying the precipitate with acetone. The powder thus obtained was extracted with buffer and was subjected to chromatographic and electrophoretic procedures as follows: (a) ammo...
Porcine pancreatic RNase was isolated from the pancreatic secretion of animals with permanent fistulas by a combination of DEAE-cellulose chromatography, adsorption-elution from sulfoethyl-Sephadex, and gel filtration on Sephadex G-100. On the basis of these experiments, a practicable, large scale procedure was developed for the preparation of the enzyme in quantities of 100 to 200 mg. Porcine ...
A method is described for the rapid preparation of electrophoretically pure troponin C from rabbit skeletal-muscle myofibrils that avoids the use of urea. The three-step procedure includes extraction od the myofibrils with EDTA-containing buffers, one-step elution from DEAE-Sephadex and Sephadex G-100 chromatography in the presence of EDTA. The procedure gives yields comparable with those of cu...
A cytokinin-binding protein has been isolated from wheat germ via ammonium sulfate precipitation, carboxymethyl Sephadex chromatography, and affinity chromatography on a column substituted with a derivative of kinetin riboside. On Sephadex G-200, the protein migrated with an apparent molecular weight of 122,000 daltons. The dissociation constant for kinetin was determined by equilibrium dialysi...
The purification from bovine pituitary gland of a growth factor responsible for the control of animal cell division in tissue culture is reported. This growth factor is a polypeptide of 13,300 molecular weight and is homogeneous when analyzed by polyacrylamide gel electrophoresis, carboxymethyl-Sephadex gradient elution chromatography, and Sephadex G-50 chromatography. The yield of growth facto...
Rabbit testis contains a single molecular form of proacrosin which could be extracted at acid pH and purified 145-fold by Sephadex G-100, SE-Sephadex, and concanavalin A-Sepharose affinity column chromatography. The purified proacrosin was judged to be homogeneous on the basis of chromatographic analyses, disc and sodium dodecyl sulfate-polyacrylamide disc gel electrophoresis, and immunodiffusi...
Several strains of Staphylococcus aureus and Staphylococcus epidermidis, exhibiting characteristic resistance patterns to aminoglycoside antibiotics, were examined. The aminoglycoside-modifying enzymes from these strains were purified by DEAE-Sephadex A-50 chromatography, affinity chromatography, and Sephadex G-100 gel filtration. Three enzymes, a 3'-phosphotransferase III (molecular weight, 31...
The enzyme anthranilate-5-phosphoribosylpyrophosphate phosphoribosyltransferase from Serratia marcescens was purified to apparent homogeneity. The purification procedure included ammonium sulfate precipitation, DEAE-cellulose chromatography, Sephadex gel filtration and hydroxyapatite chromatography. The molecular weight of the native protein as determined on a calibrated Sephadex G-200 column w...
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