scholarly journals The isolation and partial sequence of peptides produced by cyanogen bromide cleavage of calf thymus non-histone chromosomal high-mobility-group protein 2. Sequence homology with non-histone chromosomal high-mobility-group protein 1

1979 ◽  
Vol 181 (3) ◽  
pp. 659-665 ◽  
Author(s):  
J M Walker ◽  
K Gooderham ◽  
E W Johns
Keyword(s):  
Sequence Homology ◽  
Sequence Data ◽  
High Mobility ◽  
High Mobility Group ◽  
Peptide Sequence ◽  
British Library ◽  
Published Data ◽  
Chromosomal Protein ◽  
High Mobility Group Protein ◽  
Group Protein

Peptides produced by CNBr cleavage of non-histone chromosomal protein HMG 2 (CNBr peptides) were isolated and characterized, and their partial sequences were determined. The present sequence data account for over half of the sequence of the protein HMG (high-mobility-group) 2 molecule, and, together with previously published results, provide interesting information on the charge distribution within the molecule. Comparison of the CNBr-peptide-sequence data for protein HMG 2 with the previously published data on the CNBr peptides from protein HMG 1 reveals extensive sequence homology between the two proteins. Detailed evidence for the amino acid-sequence data has been deposited as Supplementary Publication SUP 50095 (6 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1978) 169, 5.

scholarly journals Detection of monoclonal antibody to high-mobility-group protein 17 from chick oviduct

1982 ◽  
Vol 203 (2) ◽  
pp. 471-476 ◽  
Author(s):  
C S Teng ◽  
C T Teng ◽  
T S Chan
Keyword(s):  
Solid Phase ◽  
Protein A ◽  
High Mobility ◽  
High Mobility Group ◽  
Chromosomal Protein ◽  
Hmg Proteins ◽  
High Mobility Group Protein ◽  
Group Protein ◽  
Solid Phase Radioimmunoassay ◽  
Hmg Protein

Total chromosomal HMG (high-mobility-group) proteins have been isolated from oestrogen-stimulated chick oviduct. The antibodies against these proteins were induced in mice and subsequently their spleen cells were fused with myeloma cells to form hybridomas. A highly purified HMG protein, 17, was used to select for the hybridomas that produce antibody against HMG protein 17. The hybridomas were cultured and injected into mice to produce ascites. The antibody against HMG protein 17 in the IgG (immunoglobulin G) fraction of the ascites fluid was obtained by Protein A-Sepharose column chromatography. We have devised a solid-phase radioimmunoassay and enzyme-linked serological assay for the detection and characterization of this antibody directed against HMG protein 17. This anti-(HMG protein 17) IgG interacted only with HMG protein 17, but not with other chromosomal proteins, e.g. histone H1, ‘95K protein’ (a chick oviduct-specific chromosomal protein) and HMG proteins 1, 2 and 14. The monospecific nature of this anti-(HMG protein 17) IgG fraction is confirmed.

scholarly journals Characterization of high mobility group protein levels during spermatogenesis in the rat.

1984 ◽  
Vol 259 (14) ◽  
pp. 8840-8846
Author(s):  
L R Bucci ◽  
W A Brock ◽  
I L Goldknopf ◽  
M L Meistrich
Keyword(s):  
High Mobility ◽  
High Mobility Group ◽  
High Mobility Group Protein ◽  
Protein Levels ◽  
Group Protein

scholarly journals High Mobility Group Protein B1 Is an Activator of Apoptotic Response to Antimetabolite Drugs

2007 ◽  
Vol 73 (1) ◽  
pp. 260-269 ◽  
Author(s):  
Natalia Krynetskaia ◽  
Hongbo Xie ◽  
Slobodan Vucetic ◽  
Zoran Obradovic ◽  
Evgeny Krynetskiy
Keyword(s):  
High Mobility ◽  
High Mobility Group ◽  
Apoptotic Response ◽  
High Mobility Group Protein ◽  
Group Protein
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