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 Changes in quantities of high-mobility-group protein 1 in oviduct cellular fractions after oestrogen stimulation

1981 ◽  
Vol 198 (1) ◽  
pp. 85-90 ◽  
Author(s):  
C T Teng ◽  
C S Teng
Keyword(s):  
Microsomal Fraction ◽  
High Mobility ◽  
Quantitative Change ◽  
High Mobility Group ◽  
Nuclear Fraction ◽  
Hmg Proteins ◽  
High Mobility Group Protein ◽  
Group Protein ◽  
Oviduct Cell

Antiserum against chick oviduct high-mobility-group protein 1 (HMG 1) has been induced in the rabbit. With this antiserum, immunobiochemical techniques have been used to probe the quantitative change of HMG 1 in the cellular fractions of chick oviduct before or after oestrogen stimulation. HMG 1 is detectable in the cytosol, microsomal and nuclear fraction of the chick oviduct cell. After administration of oestrogen to young chicks in vivo for 5 days, the quantity of HMG 1 is increased 4-fold in the cytosol, 3.5-fold in the microsomal fraction and 1.6-fold in the nuclear fraction. The finding of large amounts of HMG 1 in cytoplasm of oviduct cell is not likely due to its leakage from the nucleus. We anticipate that HMG 1 is synthesized in the cytoplasm and then transported into the nucleus. The synthesis and transportation of HMG proteins is probably regulated by oestrogen.

scholarly journals A high-mobility-group protein and its cDNAs from Drosophila melanogaster.

1992 ◽  
Vol 12 (5) ◽  
pp. 1915-1923 ◽  
Author(s):  
C R Wagner ◽  
K Hamana ◽  
S C Elgin
Keyword(s):  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Acid Content ◽  
Amino Acid Content ◽  
High Mobility ◽  
High Mobility Group ◽  
Chromosome 2 ◽  
Hmg Proteins ◽  
High Mobility Group Protein ◽  
Hmg Protein

We have identified, purified, and characterized a high-mobility-group (HMG) protein and its cDNAs from Drosophila melanogaster. This protein, HMG D, shares most of the characteristics of vertebrate HMG proteins; it is extractable from nuclei with 0.35 M NaCl, is soluble in 5% perchloric acid, is relatively small (molecular weight of 12,000), has both a high basic (24%) and high acidic (24%) amino acid content, and is a DNA-binding protein. HMG D exhibits characteristics of both the vertebrate HMG 1 and 2 class and the HMG 14 and 17 class of proteins. Its amino acid sequence is similar (36% amino acid identity) to that of HMG1, while its size and selective extraction with ethidium bromide are similar to properties of the HMG 14 and 17 class of proteins. HMG D is encoded by a single-copy gene that maps to 57F8-11 on the right arm of chromosome 2. Two transcripts are observed during embryogenesis; the protein is relatively stable throughout development. By the biochemical criteria of size, solubility, and amino acid content, HMG D appears to be the major HMG protein of D. melanogaster.

Preferential Phosphorylation of High Mobility Group Protein 17 in vitro by a Nuclear Protein Kinase

1981 ◽  
Vol 36 (3-4) ◽  
pp. 319-322 ◽  
Keyword(s):  
Nuclear Protein ◽  
High Mobility ◽  
High Specificity ◽  
High Mobility Group ◽  
Hmg Proteins ◽  
High Mobility Group Protein ◽  
High Preference ◽  
Group Protein

The ability of the high mobility group proteins (HMG-1,2,14 and 17) to serve as substrate for protein kinases was investigated by incubating them with a cytoplasmic and nuclear kinase. In both cases phosphate was incorporated into all four HMG proteins. The amount of phosphate incorporated and the specificity for the four proteins was quite different for the two kinases. Whereas the cytoplasmic kinase phosphorylated the HMG-1 and 2 to a higher degree than HMG-14 and 17, the nuclear kinase exhibited a high specificity for the HMG -17, leaving the other three proteins with only a small amount. The high preference of a nuclear kinase for HMG-17 may be indicative of a specific phosphorylation occuring also in vivo

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.

Role of High-mobility Group Protein A Isoforms and Their Clinicopathologic Significance in Primary Retinoblastoma

2017 ◽  
Vol 25 (4) ◽  
pp. 244-250 ◽  
Author(s):  
Mithalesh K. Singh ◽  
Lata Singh ◽  
Seema Sen ◽  
Neelam Pushker ◽  
Anjana Sharma ◽  
...  
Keyword(s):  
Protein A ◽  
High Mobility ◽  
High Mobility Group ◽  
High Mobility Group Protein ◽  
Group Protein

High-mobility group protein HMGB2 regulates human erythroid differentiation through trans-activation of GFI1B transcription

Blood ◽  
2010 ◽  
Vol 115 (3) ◽  
pp. 687-695 ◽  
Author(s):  
Benoît Laurent ◽  
Voahangy Randrianarison-Huetz ◽  
Vincent Maréchal ◽  
Patrick Mayeux ◽  
Isabella Dusanter-Fourt ◽  
...  
Keyword(s):  
High Mobility ◽  
Erythroid Differentiation ◽  
High Mobility Group ◽  
Hematopoietic Progenitor Cells ◽  
Hematopoietic Progenitor ◽  
High Mobility Group Protein ◽  
Group Protein ◽  
Hmg Protein ◽  
Embryonic Death

Abstract Gfi-1B is a transcriptional repressor that is crucial for erythroid differentiation: inactivation of the GFI1B gene in mice leads to embryonic death due to failure to produce differentiated red cells. Accordingly, GFI1B expression is tightly regulated during erythropoiesis, but the mechanisms involved in such regulation remain partially understood. We here identify HMGB2, a high-mobility group HMG protein, as a key regulator of GFI1B transcription. HMGB2 binds to the GFI1B promoter in vivo and up-regulates its trans-activation most likely by enhancing the binding of Oct-1 and, to a lesser extent, of GATA-1 and NF-Y to the GFI1B promoter. HMGB2 expression increases during erythroid differentiation concomitantly to the increase of GfI1B transcription. Importantly, knockdown of HMGB2 in immature hematopoietic progenitor cells leads to decreased Gfi-1B expression and impairs their erythroid differentiation. We propose that HMGB2 potentiates GATA-1–dependent transcription of GFI1B by Oct-1 and thereby controls erythroid differentiation.

scholarly journals A high-mobility-group protein and its cDNAs from Drosophila melanogaster

1992 ◽  
Vol 12 (5) ◽  
pp. 1915-1923
Author(s):  
C R Wagner ◽  
K Hamana ◽  
S C Elgin
Keyword(s):  
Drosophila Melanogaster ◽  
Amino Acid ◽  
Acid Content ◽  
Amino Acid Content ◽  
High Mobility ◽  
High Mobility Group ◽  
Chromosome 2 ◽  
Hmg Proteins ◽  
High Mobility Group Protein ◽  
Hmg Protein

We have identified, purified, and characterized a high-mobility-group (HMG) protein and its cDNAs from Drosophila melanogaster. This protein, HMG D, shares most of the characteristics of vertebrate HMG proteins; it is extractable from nuclei with 0.35 M NaCl, is soluble in 5% perchloric acid, is relatively small (molecular weight of 12,000), has both a high basic (24%) and high acidic (24%) amino acid content, and is a DNA-binding protein. HMG D exhibits characteristics of both the vertebrate HMG 1 and 2 class and the HMG 14 and 17 class of proteins. Its amino acid sequence is similar (36% amino acid identity) to that of HMG1, while its size and selective extraction with ethidium bromide are similar to properties of the HMG 14 and 17 class of proteins. HMG D is encoded by a single-copy gene that maps to 57F8-11 on the right arm of chromosome 2. Two transcripts are observed during embryogenesis; the protein is relatively stable throughout development. By the biochemical criteria of size, solubility, and amino acid content, HMG D appears to be the major HMG protein of D. melanogaster.

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