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The complete amino acid sequence of human complex-forming glycoprotein heterogeneous in charge (protein HC) from one individual

López Otin, C ; Grubb, A O LU orcid and Méndez, E (1984) In Archives of Biochemistry and Biophysics 228(2). p.54-544
Abstract

The complete amino acid sequence of the single polypeptide chain of human complex-forming glycoprotein heterogeneous in charge (protein HC) isolated from a single individual is reported with the supporting data. The primary structure was determined by automatic degradation of the intact chain and of fragments obtained by chemical and enzymatic degradations of the native or reduced and S-carboxymethylated protein. The polypeptide chain of protein HC contained 182 amino acid residues with a calculated molecular weight of 20,621. No amino acid sequence variability was found and such variability can therefore not explain the great charge heterogeneity of protein HC in a single individual. The amino acid sequence of protein HC was nearly... (More)

The complete amino acid sequence of the single polypeptide chain of human complex-forming glycoprotein heterogeneous in charge (protein HC) isolated from a single individual is reported with the supporting data. The primary structure was determined by automatic degradation of the intact chain and of fragments obtained by chemical and enzymatic degradations of the native or reduced and S-carboxymethylated protein. The polypeptide chain of protein HC contained 182 amino acid residues with a calculated molecular weight of 20,621. No amino acid sequence variability was found and such variability can therefore not explain the great charge heterogeneity of protein HC in a single individual. The amino acid sequence of protein HC was nearly identical to the one reported for human alpha 1-microglobulin in a research communication but contained 15 additional residues.

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author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Alpha-Globulins/isolation & purification, Amino Acid Sequence, Chemical Phenomena, Chemistry, Humans, Peptide Fragments
in
Archives of Biochemistry and Biophysics
volume
228
issue
2
pages
54 - 544
publisher
Academic Press
external identifiers
  • pmid:6198962
  • scopus:0021378615
ISSN
0003-9861
DOI
10.1016/0003-9861(84)90021-3
language
English
LU publication?
yes
id
efff95f2-2d6b-4972-9538-d6d9ccf012b5
date added to LUP
2021-10-25 11:57:33
date last changed
2024-03-22 16:24:58
@article{efff95f2-2d6b-4972-9538-d6d9ccf012b5,
  abstract     = {{<p>The complete amino acid sequence of the single polypeptide chain of human complex-forming glycoprotein heterogeneous in charge (protein HC) isolated from a single individual is reported with the supporting data. The primary structure was determined by automatic degradation of the intact chain and of fragments obtained by chemical and enzymatic degradations of the native or reduced and S-carboxymethylated protein. The polypeptide chain of protein HC contained 182 amino acid residues with a calculated molecular weight of 20,621. No amino acid sequence variability was found and such variability can therefore not explain the great charge heterogeneity of protein HC in a single individual. The amino acid sequence of protein HC was nearly identical to the one reported for human alpha 1-microglobulin in a research communication but contained 15 additional residues.</p>}},
  author       = {{López Otin, C and Grubb, A O and Méndez, E}},
  issn         = {{0003-9861}},
  keywords     = {{Alpha-Globulins/isolation & purification; Amino Acid Sequence; Chemical Phenomena; Chemistry; Humans; Peptide Fragments}},
  language     = {{eng}},
  number       = {{2}},
  pages        = {{54--544}},
  publisher    = {{Academic Press}},
  series       = {{Archives of Biochemistry and Biophysics}},
  title        = {{The complete amino acid sequence of human complex-forming glycoprotein heterogeneous in charge (protein HC) from one individual}},
  url          = {{http://dx.doi.org/10.1016/0003-9861(84)90021-3}},
  doi          = {{10.1016/0003-9861(84)90021-3}},
  volume       = {{228}},
  year         = {{1984}},
}