1973
DOI: 10.1111/j.1432-1033.1973.tb02773.x
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Amino‐Acid Sequence of a Peptide from Human‐Serum Albumin

Abstract: A peptide obtained by cleavage of human serum albumin with cyanogen bromide was isolated by gel filtration and ion-exchange chromatography. The peptide contains 31 amino acids and has proline as its amino terminal residue. The amino acid sequence of this peptide has been determined by conventional methods.

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Cited by 9 publications
(3 citation statements)
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“…The data on the cyanogen bromide fragments of human serum albumin published by McMenamy et al [7] are in good agreement with our results [12,14,16], as well as the data of Lapresle and Bellon [30] on the order of two of the cyanogen bromide fragments. The information of Babin and Goose [9] on the sequence of residues 299-329 of our structure ( fig.2) also corresponds to our data. The so far most complete sequence data on human serum albumin have been published in a preliminary report by Behrens et al [lo].…”
Section: Resultssupporting
confidence: 87%
See 1 more Smart Citation
“…The data on the cyanogen bromide fragments of human serum albumin published by McMenamy et al [7] are in good agreement with our results [12,14,16], as well as the data of Lapresle and Bellon [30] on the order of two of the cyanogen bromide fragments. The information of Babin and Goose [9] on the sequence of residues 299-329 of our structure ( fig.2) also corresponds to our data. The so far most complete sequence data on human serum albumin have been published in a preliminary report by Behrens et al [lo].…”
Section: Resultssupporting
confidence: 87%
“…In 1970 we began in this Laboratory systematic studies of human serum albumin aimed at the determination of the complete amino acid sequence of the protein. The primary structure of human serum albumin was concurrently studied also at the University of Buffalo [6,8], at Craighton University Medical School [9], and at the University of Texas [IO]. This paper reports on the complete amino acid sequence of human serum albumin, including the positions of all amides; the results presented are confronted with sequential data reported from other laboratories.…”
Section: Introductionmentioning
confidence: 99%
“…11. The inside ring of numbers (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18) indicates the sequence positions of residues along the helix. simply based on a helix conformation running down from the two Cys residues that close the large loop by a disulfide bond.…”
Section: Origin Of the Primordial Subdomainmentioning
confidence: 99%