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Human complex-forming glycoprotein, heterogeneous in charge : the primary structure around the cysteine residues and characterization of a disulfide bridge

Mendez, E ; Grubb, A O LU orcid ; Lopez, C ; Frangione, B and Franklin, E C (1982) In Archives of Biochemistry and Biophysics 213(1). p.50-240
Abstract
The amino acid sequence of the cysteine-containing regions of human complex-forming glycoprotein, heterogeneous in charge (protein HC) was determined by studies of the tryptic peptides of the completely reduced and radioalkylated protein. One of the cysteines was located in the amino-terminal part of the molecule at position 34....
Diagonal map electrophoresis showed that the cysteine residue in the carboxy-terminal region was bridged to the cysteine containing sequence in the middle of the molecule. The function of the cysteine residue at position 34 remains elusive since the residue was not found on the diagonal maps. The release of cysteic acid and a small cysteic acid containing peptide after oxidation of the native protein HC... (More)
The amino acid sequence of the cysteine-containing regions of human complex-forming glycoprotein, heterogeneous in charge (protein HC) was determined by studies of the tryptic peptides of the completely reduced and radioalkylated protein. One of the cysteines was located in the amino-terminal part of the molecule at position 34....
Diagonal map electrophoresis showed that the cysteine residue in the carboxy-terminal region was bridged to the cysteine containing sequence in the middle of the molecule. The function of the cysteine residue at position 34 remains elusive since the residue was not found on the diagonal maps. The release of cysteic acid and a small cysteic acid containing peptide after oxidation of the native protein HC molecule suggests that this cysteine residue may be involved in disulfide bridges with cysteine and small cysteine containing peptides. (Less)
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author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Alpha-Globulins/analysis, Amino Acid Sequence, Chromatography, Gel, Cyanogen Bromide, Cysteine/analysis, Humans, Trypsin/metabolism
in
Archives of Biochemistry and Biophysics
volume
213
issue
1
pages
50 - 240
publisher
Academic Press
external identifiers
  • pmid:6174078
  • scopus:0020013957
ISSN
0003-9861
DOI
10.1016/0003-9861(82)90458-1
language
English
LU publication?
yes
id
6690cd59-1c35-4d59-9c76-afc5d38b3806
date added to LUP
2021-10-22 15:25:05
date last changed
2024-01-12 02:57:58
@article{6690cd59-1c35-4d59-9c76-afc5d38b3806,
  abstract     = {{The amino acid sequence of the cysteine-containing regions of human complex-forming glycoprotein, heterogeneous in charge (protein HC) was determined by studies of the tryptic peptides of the completely reduced and radioalkylated protein. One of the cysteines was located in the amino-terminal part of the molecule at position 34....<br/>Diagonal map electrophoresis showed that the cysteine residue in the carboxy-terminal region was bridged to the cysteine containing sequence in the middle of the molecule. The function of the cysteine residue at position 34 remains elusive since the residue was not found on the diagonal maps. The release of cysteic acid and a small cysteic acid containing peptide after oxidation of the native protein HC molecule suggests that this cysteine residue may be involved in disulfide bridges with cysteine and small cysteine containing peptides.}},
  author       = {{Mendez, E and Grubb, A O and Lopez, C and Frangione, B and Franklin, E C}},
  issn         = {{0003-9861}},
  keywords     = {{Alpha-Globulins/analysis; Amino Acid Sequence; Chromatography, Gel; Cyanogen Bromide; Cysteine/analysis; Humans; Trypsin/metabolism}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{50--240}},
  publisher    = {{Academic Press}},
  series       = {{Archives of Biochemistry and Biophysics}},
  title        = {{Human complex-forming glycoprotein, heterogeneous in charge : the primary structure around the cysteine residues and characterization of a disulfide bridge}},
  url          = {{http://dx.doi.org/10.1016/0003-9861(82)90458-1}},
  doi          = {{10.1016/0003-9861(82)90458-1}},
  volume       = {{213}},
  year         = {{1982}},
}