scholarly journals Separation of a series of chromophores and fluorophores present in elastin

1975 ◽  
Vol 147 (2) ◽  
pp. 215-219 ◽  
Author(s):  
D P Thornhill
Keyword(s):  
Optical Properties ◽  
Ion Exchange ◽  
Fluorescence Spectra ◽  
Cation Exchanger ◽  
Gel Permeation Chromatography ◽  
Protein Molecule ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Intact Protein ◽  
Gel Permeation

Purified elastin was hydrolysed with HCl and manipulated under conditions that minimized oxidation. Gel-permeation chromatography on polyacrylamide gel and ion-exchange chromatography on dextran cation-exchanger each resulted in the separation of a series of yellow fluorescent fractions. These hitherto unreported ampholytes have fluorescence spectra that approximate to that of the intact protein, and account for its characteristic optical properties. Since the coloured fluorophores are confined to enzyme-resistant regions of the protein molecule they appear to have important structural implications.

Quantitative fractionation of casein mixtures by fast protein liquid chromatography

1987 ◽  
Vol 54 (3) ◽  
pp. 369-376 ◽  
Author(s):  
D. Thomas Davies ◽  
Andrew J. R. Law
Keyword(s):  
Liquid Chromatography ◽  
Ion Exchange ◽  
Deae Cellulose ◽  
Gel Permeation Chromatography ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Fast Protein Liquid Chromatography ◽  
Good Resolution ◽  
Gel Permeation

SummaryAlkylation of whole casein samples by reaction with cysteamine and cystamine in a bis-tris-propane–urea buffer (pH 7·0) followed by fast protein liquid chromatography (FPLC) at 20°C on a Mono Q HR5/5 column in the same buffer and using a NaCl gradient led to good resolution of the whole casein into fractions representing (i) γ2- plus γ3-caseins, (ii) κ-caseins, (iii) β-casein, (iv) αs2-caseins and (v) αsl-caseins, together with small amounts of unidentified materials. Quantitatively the FPLC values agreed well with those for αs1-, β-, αs2- and γ2- plus γ3-caseins obtained by ion-exchange chromatography on DEAE cellulose, Whatman DE52 and with those for º-caseins obtained by gel-permeation chromatography on Sephadex G–150.

Notizen: Über das Vorkom men von Acetylcholinesterase (E.C. 3.1.1.7) in der H äm olym phe der Miesmuschel Mytilus edulis / Occurrence of an Acetylcholinesterase (E.C. 3.1.1.7) in the Haemolymph of the Mussel Mytilus edulis

1976 ◽  
Vol 31 (5-6) ◽  
pp. 333-334 ◽  
Author(s):  
Dettmar von Wachtendonk
Keyword(s):  
Ion Exchange ◽  
Mytilus Edulis ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Gel Permeation

Abstract A Cholinesterase deriving from the hemolymph of the mussel Mytilus edulis was partially purified by use of gel-permeation and ion-exchange chromatography; the specifity to different substrates or inhibitors indicates clearly the occurrence of a “true” acetylcholinesterase.

scholarly journals Two linkage-region fragments isolated from skeletal keratan sulphate contain a sulphated N-acetylglucosamine residue

1990 ◽  
Vol 269 (1) ◽  
pp. 55-59 ◽  
Author(s):  
J M Dickenson ◽  
T N Huckerby ◽  
I A Nieduszynski
Keyword(s):  
Gel Permeation Chromatography ◽  
Anion Exchange Chromatography ◽  
Ester Group ◽  
Intervertebral Discs ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Keratan Sulphate ◽  
Linkage Region ◽  
Gel Permeation ◽  
Electron Micro Probe Analysis

Peptido-keratan sulphate fragments were isolated from the nucleus pulposus of bovine intervertebral discs (6-year-old animals) after chondroitin ABC lyase digestion followed by digestion of A1D1 proteoglycans by diphenylcarbamoyl chloride-treated trypsin and gel-permeation chromatography on Sepharose CL-6B. Treatment of these peptido-keratan sulphate fragments with alkaline NaB3H4 yielded keratan sulphate chains with [3H]galactosaminitol end-labels, and these chains were further purified by gel-permeation chromatography on Sephadex G-50 and ion-exchange chromatography on a Pharmacia Mono-Q column in order to exclude any contamination with O-linked oligosaccharides. The chains were then treated with keratanase, and the digest was chromatographed on a Bio-Gel P-4 column followed by anion-exchange chromatography on a Nucleosil 5 SB column. Two oligosaccharides, each representing 18% of the recovered radiolabel, were examined by 500 MHz 1H-n.m.r. spectroscopy, and shown to have the following structures: [formula: see text] The structure of oligosaccharide (I) confirms the N-acetylneuraminylgalactose substitution at position 3 of N-acetylgalactosamine in the keratan sulphate-protein linkage region found by Hopwood & Robinson [(1974) Biochem. J. 141, 57-69] but additionally shows the presence of a 6-sulphated N-acetylglucosamine. Electron micro-probe analysis specifically confirmed the presence of sulphur in this sample. This sulphate ester group differentiates the keratan sulphate linkage region from similar structures derived from O-linked oligosaccharides [Lohmander, De Luca, Nilsson, Hascall, Caputo, Kimura & Heinegård (1980) J. Biol. Chem. 255, 6084-6091].

scholarly journals Retained folates in the rat

1977 ◽  
Vol 164 (3) ◽  
pp. 601-605 ◽  
Author(s):  
P A Barford ◽  
R J Staff ◽  
J A Blair
Keyword(s):  
Folic Acid ◽  
Ion Exchange ◽  
Gel Permeation Chromatography ◽  
Exchange Chromatography ◽  
Chromatographic Behaviour ◽  
Gel Permeation

The retention of radioactivity after doses of 14C- and 3H-labelled folic acid is described. Radioactivity was retained in liver, kidney and gut of rats for some time after administration of the dose. The retained radioactivity could not be displaced by large doses of unlabelled folic acid or unlabelled 5-methyltetrahydrofolate. 14C- and 3H-labbelled folates showed similar chromatographic behaviour onion-exchange chromatography to 5-methyltetrahydrofolate, and on ion-exchange and gel-permeation chromatography to synthetic pteroylhepta-gamma-glutamate.

Studies on an Inhibitor of Plasminogen Activation in Human Serum

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner
Keyword(s):  
Ion Exchange ◽  
Human Serum ◽  
Antithrombin Iii ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Specific Adsorption ◽  
Partial Purification ◽  
Plasminogen Activation ◽  
Preparative Electrophoresis

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.

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