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2 edition of Fractionation of bovine sarcoplasmic proteins by DEAE-cellulose chromatography found in the catalog.

Fractionation of bovine sarcoplasmic proteins by DEAE-cellulose chromatography

James Henry Rampton

Fractionation of bovine sarcoplasmic proteins by DEAE-cellulose chromatography

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  • 27 Currently reading

Published .
Written in English

    Subjects:
  • Proteins -- Research.,
  • Muscles.,
  • Chromatographic analysis.

  • Edition Notes

    Statementby James Henry Rampton.
    The Physical Object
    Pagination40 leaves, bound :
    Number of Pages40
    ID Numbers
    Open LibraryOL14338489M

      Purification steps * Total Total Specific Yield protein activity activity (%) (mg) (unit ([double ([dagger])) dagger]) Crude extract Ammonium sulphate fraction DEAE-cellulose Camel liver G6PD ( M NaCl) Sephacryl S Camel liver G6PD SUMMARY— Solubility of intramuscular collagen was studied as affected by chronological maturity in 15 bovine longissimus dorsi and 15 semimembranosus muscles and as affected by post‐mortem contraction state in the semitendinosus of 7 animals. Collagen solubility decreased significantly with each advancing maturity group in both longissimus dorsi and semimembranosus muscles. Collagen. () Ioslation and Separation of HMG Proteins and Histones H1 and H5 and Core Histones by Column Chromatography on Phosphocellulose Protein Expression and Purification, 14; Hazegh-Azam M, Kim S, Masoud S, Andersson L, White F, Johnson L, Muthukrishnan S, and Reeck GR. The resulting clear supernatant was treated with ethanol to precipitate the catalytic subunits of PP1 and PP2A, which were separated by DEAE-cellulose column chromatography. The activity peak corresponding to PP1 and PP2A was pooled separately, concentrated, dialyzed, and centrifuged, and the resulting solution was stored at –80° by:

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Fractionation of bovine sarcoplasmic proteins by DEAE-cellulose chromatography by James Henry Rampton Download PDF EPUB FB2

Download Citation | Fractionation of Bovine Sarcoplasmic Proteins by DEAE‐Cellulose Chromatography | SUMMARYA Tris buffer system (starting buffer, M Tris phosphate, pH. The research described herein pertains to the development and application of a DEAE-cellulose ion exchange chromatography procedure for the fractionation of bovine sarcoplasmic proteins.

Results of preliminary experiments indicated that columns packed under pressure possessed superior fractionational qualities than did columns packed without by: 4. Fractionation of Bovine Sarcoplasmic Proteins by DEAE-Cellulose Chromatography.

Journal of Food Science30 (4), DOI: /jtbx. Saifer, ch Pascal. Immunochemical studies of human serum components obtained Cited by: The research reported herein pertains to a study of the fractionation of fresh bovine muscle proteins by ion exchange chromatography.

A KCl-phosphate buffer, pH and an ionic strength ofwas used to extract the proteins from the by: 2. The application of such a procedure for the\ud successful fractionation of bovine sarcoplasmic proteins should stimulate\ud interest and research in characterizing the changes occurring\ud in beef muscle during the post-mortem aging period.\ud The research described herein pertains to the development and\ud application of a DEAE-cellulose ion.

Results of DEAE-cellulose ion exchange chromatography of the sarcoplasmic proteins showed only minor variations in profiles between the two aging treatments. Alterations did appear with time. Heterogeneity of bovine sarcoplasmic protein fractions obtained by DEAE-cellulose ion exchange chromatography was investigated by vertical polyacrylam Author: H.J.

Petropakis, M.W. Montgomery, W.D. Davidson, A.F. Anglemier. Fraction areas I and II, eluted during the early stage of DEAE-cellulose chromatography of the sarcoplasmic proteins, correspond to the slower moving bands in the electrophoretic patterns. Such bands have a low level of electronegativity since the time required for electrophoresis decreased from 20 hr for fraction area I and 10 lir for fraction area II, to 7, 5 and 4 hr for fraction areas III, IV,and V, Author: H.J.

Petropakis, M.W. Montgomery, W.D. Davidson, A.F. Anglemier. Abstract An ion exchange chromatography process was developed to separate the main protein fractions of bovine blood plasma using a composite material, Q-HyperD resin, and a gel material, DEAE-Sepharose.

The experiments were carried out at semipreparative by: 4. Use of simple concentration gradients for the fractionation of human serum proteins on deae-cellulose, with especial reference to the isolation of albumin, prealbumin, haemopexin and transferrin.

Journal of Chromatography A84 (1), DOI: /S(01)Cited by: Hence, the development of a procedure\ud for the adequate fractionation of muscle proteins would greatly stimulate\ud the interest and research progress in this difficult field of study.\ud The research reported herein pertains to a study of the\ud fractionation of fresh bovine muscle proteins by ion exchange chromatography.\ud A KCl-phosphate.

DEAE-Cellulose Chromatography: Preparation of γG-Immunoglobulin Fractionation of Serum γG γA γM γD Quantitation of γ-G Immunoglobulin Species Differences Technical Considerations: Variability among DEAE-Celluloses Overloading with Protein Euglobulin Recovery Special Cases: Myeloma Proteins and Waldenström Macroglobulins, Bence-Jones ProteinsBook Edition: 1.

Protein Purification DEAE cellulose columns are rarely used at pH greater than Why. Protein Purification 6-phosphogluconate dehydrogenase has a pI of 6. Explain why the buffer used for a chromatography on DEAE-cellulose must have a pH greater than 6 but less than 9 in order to ensure the enzyme is efficiently bound to the column File Size: KB.

Immobilized metal affinity chromatography (IMAC) is a useful protein fractionation method used to enrich metal associated proteins. IMAC represents an affinity separation approach based on the interaction between proteins and metal ions immobilized on a solid by: 8 An example of stepwise elution protein applied to the meats field is some recent work of Fujimaki and Deatherage (28), who are inter- ested in the chromatographic fractionation of sarcoplasmic proteins of beef skeletal muscle on ion-exchange cellulose.

freshly slaughtered beef were extracted with distilled water and mg of the extract chromatographed on cellulose phosphate. Ion exchange mechanism. Ion-exchange chromatography which is designed specifically for the separation of differently charged or ionizable compounds comprises from mobile and stationary phases similar to other forms of column based liquid chromatography techniques [].Mobil phases consist an aqueous buffer system into which the mixture to be by: Chromatography in DEAE‐cellulose— The dialyzed crude extract is centrifuged at 4 °C for 10 min at 14, rpm to clarify the solution.

The supernatant, containing FNR and ferredoxin, is separated from the pellet, and the volume of this extract is measured before removing 1 ml (aliquot 2) that will be kept in the freezer for subsequent by: 9.

Since the initial description (2, 3) of procedures for the use of cellulose ion exchange columns for the chromatography of proteins, a number of such systems have been developed for specific proteins, including the heme proteins.

Thus, Gutter et al. (4) have described the use of carboxymethyl cellulose in a study of various hemoglobins, Rumen (5) has utilized carboxymethyl cellulose for the. Phosphorylation of a 22,Dalton Component of the Cardiac Sarcoplasmic Reticulum by Adenosine 3’: S-Monophosphate-dependent Protein Kinase* bilization in sodium dodecyl sulfate and fractionation by poly- acrylamide gel electrophoresis, a single microsomal protein ing sarcoplasmic reticulum ATPase protein, contained signifi.

In an effort to simplify a complex mixture of soluble proteins from Escherichia coli, methods to fractionate the samples prior to two-dimensional (2D) gel electrophoresis were developed. These methods involve the use of DEAE-Sepharose, SP-Sepharose, and phenyl Sepharose chromatographic columns and the fractionation of the protein mixtures based on differential anionic, cationic, and Cited by: sarcoplasmic reticulum Caa’-ATPase, and cytochrome oxidase was measured after equilibration and delipi- dation, both by the use of successive chromatographies on silica gel and the use of agarose gel columns in combination with DEAE-cellulose chromatography.

It was found that, despite detergent binding by silica gel. [27] Post, A.E. () Fractionation of bovine casein and enrichment of functional casein peptides.

in, University of Hohenheim, Dr. Hut, Stuttgart, Germany. [28] Post, A.E., Hinrichs, J. () Suitability of commercial caseinates in comparison to micellar casein as Cited by: 1.

Ion-exchange chromatography is widely used in biochemistry to isolate and purify protein samples. Proteins have many amino acids with functional groups that are charged. Proteins are separated based on net charge, which is dependent on pH.

Some proteins are more positively charged while others are more negatively charged. Isolated bovine cardiac SR was solubilized in a buffer containing deoxycholate and the soluble fraction was applied to the immunoaffinity column.

After washing the column with a series of detergent-containing buffer solutions, the column-bound protein which contained essentially pure phospholamban was eluted by a buffer containing M MgCl 2Cited by: 7. fractionation of plasma components such as prothrombin complex using the batch ion exchange technique, and the purification of insulin by traditional column chromatography.

Sephadex ion exchangers General description Sephadex ion exchangers are produced by introducing functional groups onto Sephadex, a cross-linked dextran matrix.

These groups are. proteins were initially found in brain tissue in and purified using chromatography and gel electrophoresis. In bovine brain samples, proteins were located in the 14th fraction eluting from a DEAE-cellulose column and in position on a starch electrophesis gel.

FunctionInterPro: IPR Bovine brain tissue, collecting, Brain (DEAE) cellulose, Diethylaminoethyl (DEAE) Sephadex, Differential centrifugation, 2–3 Discontinuous sucrose gradient preparation, membrane proteins in eluted fraction, 8–9 using immunoblots with plasma membrane markers, 9.

DEAE Cellulose chromatography at pH Active fractions eluted from sepharose-4B column were pooled and purified on a DEAE Cellulose column (12x 3cm) eluting with phosphate buffer (50mM, pH ) containing 1mM EDTA and 5mM 2-mercaptoethanol.

The enzyme was eluted with same buffer at. Separation of sarcoplasmic proteins by fractionation on Sephadex and DEAE cellulose columns indicated that a low abundance fatty acid-binding protein exists in bovine l. dorsi muscle. Fatty acid-binding protein in bovine l. dorsi muscle cannot be separated from myoglobin by standard protein purification by: 9.

The bones were frozen in liquid nitrogen and crushed into small pieces with a hydraulic press, followed by grinding of the frozen bone pieces into powder. g of frozen powdered bovine bone was extracted in sequence, first with 10 vol of 4 M guanidine hydrochloride in 50 mM sodium acetate, pH (to remove non–mineral-associated proteins Cited by: Abstract ABSTRACT.

The oxidation of myofibrillar and sarcoplasmic proteins of thin-lipped mullet (Liza ramada) in different ages during refrigerated storage (4C), and in vitro oxidation of muscle after 2 and 24 h incubation with Fe +2 /H 2 O 2 at 4C were evaluated by means of protein carbonyl s in myofibrillar and sarcoplasmic proteins were estimated by sodium dodecyl sulfate.

Solubilized protein derived from human platelets was fractionated by DEAE cellulose column chromatography and analyzed for protease activity using three substrates: denatured bovine hemoglobin, alpha casein, and purified plasminogen-free human fibrinogen.

Rat liver peroxisomes isolated by density gradient centrifugation were disrupted at pH 9, and subdivided into a soluble fraction containing 90% of their total proteins and virtually all of their catalase, D-amino acid oxidase, L-α-hydroxy acid oxidase and isocitrate dehydrogenase activities, and a core fraction containing urate oxidase and 10% of the total by: The cGMP binding protein-phosphodiesterase (cG-BPP) with a phosphodiesterase specific activity of mu.M/min/mg has been purified from rat lung by sequential chromatography on DEAE-cellulose, Blue-Sepharose, zinc chelate affinity adsorbent and HPLC-DEAE.

Migration of the major band on SDS-PAGE corresponds to a MW of approx, The sarcoplasmic reticulum (SR) is one of the major regulators of the cytosolic Ca2+ concentration in cardiac ventricular muscle cells.

In the myocardium, relaxation results from a decrease in cytoplasmic free Ca2+ levels mediated through an efflux of Ca2+ from the cell via the sarcolemmal Na+/Ca2+- exchanger and by the sequestration of 0a2+ by the network SR membranes through the actions of a.

Cirrhina mrigala has been purified 40 fold by ammonium sulphate fractionation, adsor­ ption on alumina Cs gel and chromatography using DEAE-cellulose column and the properties of the purified enzyme studied.

The pH optimum of the enzyme is The Km value of aspartic acid and 2-oxoglutaric acid are found to be x M and. Purification of protein attracts the scientists’ attention toward science inas Somnar started purification and crystallization of urease from yeast.

As years go forward, protein purification strategies updated from using dextrose passing through DEAE-cellulose and ended by affinity chromatography. In this chapter we will describe some of the concepts and the differences between Author: Hanaa E.A.

Amer. Before the eluant from the column is collected in the fraction collector: Select one: a. It is mixed with a buffer to lower the ion concentration. It passes through a spectrophotometer. It is heated for a short period and sterilized.

It is first collected in a large cylinder and. protein 1 has a molecular weight ofkD and protein 2 kD, which protein will elute first from a saphadex GAcolumn (fractionation range for protein, D) both proteins In all type of chromatography, the mobile phase may be.

The glycome of bovine milk proteins. There are two types of protein glycosylation present in bovine milk: N-linked, where the glycan chain is covalently linked via an N-acetyl glucosamine molecule to the amide side chain of an asparagine residue, and O-linked, where the glycan chain is covalently attached to the hydroxyl oxygen of a serine or threonine residue (Vance et al.

).Cited by:. Fed-batch Fermentation is primarily a practical guide for recombinant protein production in E. coli using a Fed-batch Fermentation process. Ideal users of this guide are teaching labs and R&D labs that need a quick and reproducible process for recombinant protein : [email protected]{osti_, title = {Protein degradation in Euglena gracilis: Purification and characterization of the major proteinase}, author = {Yoo, Y J}, abstractNote = {Protolysis in a crude extract of Euglena gracilis was characterized by autolysis and the hydrolysis of {sup }I-labeled bovine serum albumin ({sup }I-BSA).

Both procedures showed similar properties: stimulation by.The eluting buffer was collected with a fraction collector, and the protein content of each fraction was estimated by measurements • Upon chromatography of the crude inhibitor preparation on the 12 tryps in-Sepharose 4B column, inactive proteins and pigmented mater- ial did not bind to the column and were washed from the column by the.