Separation of Polypeptides bound by Albumin in Human Plasma

Rubin, Albert L.; Lubash, Glenn D.; Aronson, Ruth F.; Davison, Peter F.

doi:10.1038/1971009a0

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1964

1991

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Cited by 13 publications

(2 citation statements)

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“…(1961). Rubin et al (1963) have drawn attention to the association of peptide-like material with the albumin fraction of human plasma.…”

Section: Discussionmentioning

confidence: 99%

Peptide-Protein Interaction as Studied by Gel Filtration^*

Fairclough¹,

Fruton²

1966

Biochemistry

179

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“…(1961). Rubin et al (1963) have drawn attention to the association of peptide-like material with the albumin fraction of human plasma.…”

Section: Discussionmentioning

confidence: 99%

Peptide-Protein Interaction as Studied by Gel Filtration^*

Fairclough¹,

Fruton²

1966

Biochemistry

179

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“…A possible candidate is peptides containing several amino-acids which are known to exist in the serum in bound and free forms (Rubin et al, 1963). It has been shown that some synthetic dipeptides, in particular L-phenylalanyl-L-19 JUNE 1971 679 phenylalanine, bind strongly to human serum proteins in vitro and are displaced by all the commonly used antirheumatic drugs (McArthur et al, 1971).…”

Section: Discussionmentioning

confidence: 99%

Mode of Action of Antirheumatic Drugs

McArthur¹,

Dawkins²,

Smith³

et al. 1971

BMJ

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Studies on the development of mouse embyros in vitro. III. The effect of fixed‐nitrogen source

Brinster

1965

J. Exp. Zool.

104

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There has been considerable discussion as to whether the developing mouse ova requires a n exogenous protein supply. A series of experiments were performed to determine the effect of various fixed-nitrogen sources on the development in vitro of two-cell mouse ova into blastocysts. It was found that two-cell mouse ova would not develop into blastocysts in medium that did not contain a hed-nitrogen source. Crystalline bovine serum albumin (BSA) at 1 mg/ml or, alternatively, the constituent amino acids of BSA could supply this requirement for fixed-nitrogen. In the presence of single amino acids at M, only an occasional twocell ova developed into a blastocyst.Single amino acids were omitted from the medium containing the constituent amino acids of BSA in a n attempt to demonstrate an essential amino acid requirement of two-cell mouse ova. The omission of no singIe amino acid from the medium, completely prevented the development of some two-cell ova into blastocysts. The only amino acid whose omission resulted in a significant decrease in development was cystine. In the medium where amino acids were used in place of BSA, a non-protein polymer was used to replace the physical properties of albumin. The non-protein polymers which appeared best were Polyvinylpyrrolidone (MW = 150,000), Acacia, Dextran, and Ficoll.

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Separation of Polypeptides bound by Albumin in Human Plasma

Cited by 13 publications

References 5 publications

Peptide-Protein Interaction as Studied by Gel Filtration^*

Peptide-Protein Interaction as Studied by Gel Filtration^*

Mode of Action of Antirheumatic Drugs

Studies on the development of mouse embyros in vitro. III. The effect of fixed‐nitrogen source

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Separation of Polypeptides bound by Albumin in Human Plasma

Cited by 13 publications

References 5 publications

Peptide-Protein Interaction as Studied by Gel Filtration*

Peptide-Protein Interaction as Studied by Gel Filtration*

Mode of Action of Antirheumatic Drugs

Studies on the development of mouse embyros in vitro. III. The effect of fixed‐nitrogen source

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Product

Resources

About

Peptide-Protein Interaction as Studied by Gel Filtration^*

Peptide-Protein Interaction as Studied by Gel Filtration^*