Chromatography of Proteins. II. Fractionation of Serum Protein on Anion-exchange Cellulose

Sober, Herbert A.; Gutter, Frederick J.; Wyckoff, Mary; Peterson, Elbert A.

doi:10.1021/ja01585a017

Cited by 656 publications

(132 citation statements)

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“…method of Sober et al (23). One group of five rabbits received 9 pS0 units of slow 7S antibody 1 day after 2 nag KLH and another group of five received 9 ps0 units of fast 7S antibody.…”

mentioning

confidence: 99%

The Effect of Passively Administered Antibody on Antibody Synthesis

Dixon

Jacot-Guillarmod

McConahey

1967

The Journal of Experimental Medicine

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Suppression of the primary response of rabbits to intravenously administered KLH can be achieved with very small amounts of hyperimmune anti-KLH administered a day later since the rabbit apparently rapidly eliminates most of the KLH by nonimmunologic means. The amount of passive anti-KLH needed to achieve immunosuppression was directly proportional to the dose of injected antigen. Antibody passively administered as much as 6–8 days after antigen still can be strongly immunosuppressive, which suggests that the antibody must be reacting with immunogen in or on responding cells or perhaps in the process of transfer between cells. There was no evidence that the presence of passively administered hyperimmune anti-KLH prior to the injection of antigen had any immunosuppressive action beyond the direct neutralization of the injected antigen. When KLH was injected in Freund adjuvant, anti-KLH incorporated with the KLH in the adjuvant was much more efficient in causing immunosuppression than anti-KLH given intravenously. The primary responses to 2 mg KLH given intravenously and 2 µg given in adjuvant reached approximately equal peaks and were suppressible by comparable amounts of intravenously administered anti-KLH. Two observations suggest that passive antibody neutralizes the immunogenic stimulus at the level of individual antigenic determinants and not merely by aggregating or precipitating entire antigenic molecules. First, anti-abalone hemocyanin (AH) which cross-reacts approximately 50% with KLH was only partially immunosuppressive even in extremely large amounts, i.e., amounts which could react with and precipitate much more KLH than could the smaller but more suppressive doses of anti-KLH. Second, when KLH and anti-KLH were given together in adjuvant, effective immunosuppression was achieved only with amounts of anti-KLH sufficient to saturate or cover virtually all available antigenic determinants. The immunosuppressive quality of passive antibody increases with time after immunization and with repeated immunization of the donor. In view of their relatively weak immunosuppressive properties, antibodies formed in the first weeks of a primary response may not contribute significantly to the turning off of the antibody response. In any event, results obtained by passive transfer of hyperimmune antibody to animals early in a primary response cannot be applied to the natural events in a primary response.

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“…method of Sober et al (23). One group of five rabbits received 9 pS0 units of slow 7S antibody 1 day after 2 nag KLH and another group of five received 9 ps0 units of fast 7S antibody.…”

mentioning

confidence: 99%

The Effect of Passively Administered Antibody on Antibody Synthesis

Dixon

Jacot-Guillarmod

McConahey

1967

The Journal of Experimental Medicine

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“…Normal y-globulins were prepared from the non-immunized animals by two successive ammonium sulfate precipitations at 35% saturation followed by chromatography on DEAE-cellulose according to Sober et al 1956 [7].…”

Section: Immunochemical Methodsmentioning

confidence: 99%

Ratio of the Fab fragments I and II from goat antibodies normal γ‐globulins

Strosberg

Kanarek

1970

FEBS Letters

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“…Boardman and Partridge (1953) were able to separate neutral proteins differing in isoelectric points by only 0.6. Early reports show the application of this method to the analysis of horse and human sera (Sober et al, 1956), various enzymes and hormones (Keller et al, 1958), and egg white proteins (Rhodes et al, 1953). Mandeles (i960) used cellulose ion exchangers to analyze cabbage extracts and extracts of two different strains of E. coll.…”

Section: Ion Exchange Chromatographymentioning

confidence: 99%

“…More recent applications of the technique have been the fractionation of ribosomal proteins (Spitnik-Elson, 1964), and separation of /^-glucanases of germinated barley by phosphorylated cellu lose (Luchsinger and Richards, 1964). A large amount of information has accumulated on the application of cellulose ion exchangers to the purification of specific proteins (Sober et al, 1956). Anion exchange celluloses most com monly used are diethylaminoethyl cellulose (DEAE-cellulose) and triethylaminoethyl cellulose (TEAE-cellulose).…”

Section: Ion Exchange Chromatographymentioning

confidence: 99%

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Post‐Rigor Changes in Selected Physicochemical Properties of Myosin B Fraction of Turkey Muscle

Scharpf

Marion

Forsythe

1966

Journal of Food Science

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SUMMARY Changes in selected physicochemical properties of the myosin B fraction of turkey muscle were followed during a 44‐hr post‐rigor aging period. Sedimentation patterns of myosin B fractions prepared 48 hr after death indicated a decrease in a high‐molecular‐weight component thought to he myosin B gel. It is concluded that myosin B fractions lose gel‐forming ability with resolution of rigor. Density‐gradient centrifugal patterns showed small increases in slowly sedimenting components of myosin B fractions with aging. These components were. high in ATP‐ase activity in the presence of calcium ions and showed no reduction of viscosity with addition of ATP. Some evidence favors the concept of dissociation of myosin B into myosin A and actin with resolution of rigor. This dissociation, however, may also represent disruption of myosin R gel formed during and after extraction from muscle.

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Chromatography of Proteins. II. Fractionation of Serum Protein on Anion-exchange Cellulose

Cited by 656 publications

References 1 publication

The Effect of Passively Administered Antibody on Antibody Synthesis

The Effect of Passively Administered Antibody on Antibody Synthesis

Ratio of the Fab fragments I and II from goat antibodies normal γ‐globulins

Post‐Rigor Changes in Selected Physicochemical Properties of Myosin B Fraction of Turkey Muscle

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