Complete amino acid sequence of human serum albumin

Meloun, B.; Morávek, L.; Kostka, V.

doi:10.1016/0014-5793(75)80242-0

Cited by 389 publications

(148 citation statements)

References 18 publications

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“…As shown in Table 1, the amino acid compositions of cord and adult albumins were essentially identical. Moreover, the values were in good agreement with the known amino acid composition of adult albumin derived from the primary structure (25,26). Automatic Edman degradation yielded identical sequences for the first eight amino acid residues (Asp-Ala-His-Lys-Ser-Glu-Val-Ala-) of both albumins.…”

Section: Resultssupporting

confidence: 75%

“…3). This was confirmed by analyses of amino acid composition ( (leucine), all of which agreed with the known primary structure of adult albumin (25,26).…”

Section: Resultssupporting

confidence: 72%

“…In the presence ot NaDodSO4 both cord and adult albumin traveled as a single band with an apparent molecular weight of 69,000 (Fig. 1A), a value that approximates the known molecular weight of 66,500 (25). That both proteins had not only the same size but also the same charge was indicated by identical mobilities in polyacrylamide gels in the absence of NaDodSO4.…”

Section: Resultsmentioning

confidence: 68%

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Fetal and adult albumins are indistinguishable by immunological and physicochemical criteria

Gitzelmann-Cumarasamy

Gitzelmann²,

Wilson

et al. 1979

Proc. Natl. Acad. Sci. U.S.A.

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The existence of a functionally immature fetal albumin has been postulated to explain the reduced ability of newborn plasma to bind bilirubin and various drugs. In support of this, cord and adult albumin, isolated by a simple salting-out technique, were reported to differ in electrophoretic and chromatographic properties and in their resistance to alkali and proteolytic enzymes. However, the interpretation of these findings has since been questioned. To resolve this controversy, we have purified to homogeneity human serum albumins from pooled umbilical cord and adult donor plasma. The two albumins were compared and found to be indistinguishable by polyacrylamide gel electrophoresis with and without sodium dodecyl sulfate, as well as by immunoelectrophoresis and double immunodiffusion using specific antibodies against both albumins. Furthermore, the amino acid compositions, the aminoterminal sequence (Asp-Ala-His-Lys-Ser-Glu-Val-Ala-), the carboxy terminus (Leu), and the peptide fingerprints were identical in the two albumins. No significant differences were found by circular dichroism in the ultraviolet (200-350 nm). Binding studies with bilirubin showed association constants of 3.7 + 0.7 X 107 M-1 for cord and 2.9 : 0.3 X 107 M-' for adult albumin, respectively. The circular dichroic spectra of 1:1 bilirubin-albumin complexes showed considerable variation between the batches but were not significantly different. The only difference was found in the fluorescence spectra of the bilirubin-albumin complexes, in which complexes with adult albumin showed only 75% of the relative fluorescence exhibited with cord albumin. The combined results nevertheless strongly indicate that fetal and adult albumins are very similar, if not identical. Human serum albumin is an almost universal carrier for a host of metabolites and drugs (1). As such it plays a central role in the regulation of their activity or toxicity. This is of particular significance in neonatal medicine because newborns, with their immature detoxifying mechanisms (for review see ref.2), are highly susceptible to various toxic agents. A well-known example is bilirubin encephalopathy resulting from neonatal jaundice.During clinical studies it was observed that newborn serum has a lower ability to bind bilirubin and drugs than adult serum does (refs. 3 and 4 and references cited therein). To explain these observations, the existence of a fetal type of albumin, analogous to hemoglobin F, was postulated. In support of this, cord and adult albumin, isolated by a simple salting-out technique, were reported to differ in electrophoretic and chromatographic properties and to vary in resistance to alkali and proteolytic enzymes (5, 6). However, authors of subsequent papers questioned the existence of a functionally immature albumin and attributed the reduced binding of newborn serum to competitive binding by increased concentrations of certain metabolites such as arachidonic acid and hematin (7-11).To resolve this controversy, we purified cord and adult albumin...

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Section: Resultssupporting

confidence: 75%

“…3). This was confirmed by analyses of amino acid composition ( (leucine), all of which agreed with the known primary structure of adult albumin (25,26).…”

Section: Resultssupporting

confidence: 72%

Section: Resultsmentioning

confidence: 68%

See 1 more Smart Citation

Fetal and adult albumins are indistinguishable by immunological and physicochemical criteria

Gitzelmann-Cumarasamy

Gitzelmann²,

Wilson

et al. 1979

Proc. Natl. Acad. Sci. U.S.A.

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“…Sequence analysis bf this peptide demonstrated that radioactivity was associated with the lysine residue at position 2 of the peptide (table 1). This peptide corresponds to residues 198-205 of human serum albumin as determined by Meloun, Mor~ivek and Kostka [6]. The corresponding residue in the sequence described by Behrens et al was assigned as arginine [5].…”

Section: The Dansyl-edman Methodsmentioning

confidence: 99%

Lysine residue 199 of human serum albumin is modified by acetylsalicylic acid

Walker

1976

FEBS Letters

117

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“…11 Albumin has a high percentage of ionic amino acids, especially glutamate and lysine, which confer a relatively high solubility to the protein. As far as secondary structure is concerned, albumin is a highly helical molecule, with a a-helix content of 67%, 23% of extended chain and 10% b-turn, as determined by X-ray analysis.…”

Section: Impact Of Binding Of Drugs To Hsa On Their Pharmacokinetic Amentioning

confidence: 99%

Drug binding to human serum albumin: Abridged review of results obtained with high‐performance liquid chromatography and circular dichroism

2006

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The drug binding to plasma and tissue proteins are fundamental factors in determining the overall pharmacological activity of a drug. Human serum albumin (HSA), together with a 1 -acid glycoprotein (AGP), are the most important plasma proteins, which act as drug carriers, with drug pharmacokinetic implications, resulting in important clinical impacts for drugs that have a relatively narrow therapeutic index. This review focuses on the combination of biochromatography and circular dichroism as an effective approach for the characterization of albumin binding sites and their enantioselectivity. Furthermore, their applications to the study of changes in the binding properties of the protein arising by the reversible or covalent binding of drugs are discussed, and examples of physiological relevance reported. Perspectives of these studies reside in supporting the development of new drugs, which require miniaturization to facilitate the screening of classes of compounds for their binding to the target protein, and a deeper characterization of the mechanisms involved in the molecular recognition processes.

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Complete amino acid sequence of human serum albumin

Cited by 389 publications

References 18 publications

Fetal and adult albumins are indistinguishable by immunological and physicochemical criteria

Fetal and adult albumins are indistinguishable by immunological and physicochemical criteria

Lysine residue 199 of human serum albumin is modified by acetylsalicylic acid

Drug binding to human serum albumin: Abridged review of results obtained with high‐performance liquid chromatography and circular dichroism

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