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1988 2673
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Page 1
Showing results for kda a
Search for Keda A instead (3 results)
A 50-kDa isoform of mouse brain acyl-CoA hydrolase: expression and molecular properties.
Takagi M, Kawabe K, Suga T, Yamada J. Takagi M, et al. Arch Biochem Biophys. 2004 Sep 1;429(1):100-5. doi: 10.1016/j.abb.2004.06.005. Arch Biochem Biophys. 2004. PMID: 15288813
In addition, both 43-kDa BACH and 50-kDa BACH that were fused to green fluorescent protein showed cytosolic distribution. These results suggest that the 50-kDa BACH plays a similar role as the 43-kDa BACH. Therefore, since the 43-kDa BACH is exp …
In addition, both 43-kDa BACH and 50-kDa BACH that were fused to green fluorescent protein showed cytosolic distribution. Thes …
A possible physiological function and the tertiary structure of a 4-kDa peptide in legumes.
Yamazaki T, Takaoka M, Katoh E, Hanada K, Sakita M, Sakata K, Nishiuchi Y, Hirano H. Yamazaki T, et al. Eur J Biochem. 2003 Mar;270(6):1269-76. doi: 10.1046/j.1432-1033.2003.03489.x. Eur J Biochem. 2003. PMID: 12631285 Free article.
Previously, we isolated a 4-kDa peptide capable of binding to a 43-kDa receptor-like protein and stimulating protein kinase activity of the 43-kDa protein in soybean. ...The importance of these residues for the 4-kDa peptide to bind to the 43-kDa …
Previously, we isolated a 4-kDa peptide capable of binding to a 43-kDa receptor-like protein and stimulating protein kinase ac …
Interaction of a 43-kDa receptor-like protein with a 4-kDa hormone-like peptide in soybean.
Hanada K, Hirano H. Hanada K, et al. Biochemistry. 2004 Sep 28;43(38):12105-12. doi: 10.1021/bi049587a. Biochemistry. 2004. PMID: 15379549
A 43-kDa soybean protein is a receptor-like protein kinase that is capable of interaction with a 4-kDa hormone-like peptide (leginsulin). ...To determine the mechanism of interaction between the 4-kDa peptide and 43-kDa protein, we investigated the bin …
A 43-kDa soybean protein is a receptor-like protein kinase that is capable of interaction with a 4-kDa hormone-like peptide (l …
Detection and localization of a class of proteins immunologically related to a 100-kDa nucleolar protein.
Bugler B, Caizergues-Ferrer M, Bouche G, Bourbon H, Amalric F. Bugler B, et al. Eur J Biochem. 1982 Nov 15;128(2-3):475-80. doi: 10.1111/j.1432-1033.1982.tb06989.x. Eur J Biochem. 1982. PMID: 7151790 Free article.
In the nucleolus, four proteins with molecular masses of 100 kDa, 95 kDa, 76 kDa and 70 kDa were thus visualized. In the ribosomes, two proteins (of 100 kDa and 76 kDa) gave a strong reaction while six others (of 70 kDa, 60 kDa …
In the nucleolus, four proteins with molecular masses of 100 kDa, 95 kDa, 76 kDa and 70 kDa were thus visualized …
Isolation of a 31 kDa form of inhibin from bovine follicular fluid.
Robertson DM, de Vos FL, Foulds LM, McLachlan RI, Burger HG, Morgan FJ, Hearn MT, de Kretser DM. Robertson DM, et al. Mol Cell Endocrinol. 1986 Mar;44(3):271-7. doi: 10.1016/0303-7207(86)90133-4. Mol Cell Endocrinol. 1986. PMID: 3082696
The biological activity expressed on mg protein basis was similar for both 31 kDa and 58 kDa inhibin although on a molar basis the 58 kDa inhibin was 2-3 times higher. A high degree of cross-reaction was observed between both forms in a radioimmunoassay of bo …
The biological activity expressed on mg protein basis was similar for both 31 kDa and 58 kDa inhibin although on a molar basis …
Purification of a 190 kDa protein from smooth muscle: relationship to talin.
O'Halloran T, Burridge K. O'Halloran T, et al. Biochim Biophys Acta. 1986 Feb 14;869(3):337-49. doi: 10.1016/0167-4838(86)90074-9. Biochim Biophys Acta. 1986. PMID: 2418880
Upon prolonged storage at 4 degrees C, purified talin degrades into a 190 kDa fragment. A 190 kDa fragment is also generated from talin by the Staphylococcus aureus V-8 proteinase and by trypsin. Comparison of partial peptide maps of talin and the 190 kDa pro …
Upon prolonged storage at 4 degrees C, purified talin degrades into a 190 kDa fragment. A 190 kDa fragment is also generated f …
Autoantibody to the leucine zipper region of 52 kDa Ro/SSA binds native 60 kDa Ro/SSA: identification of a tertiary epitope with components from 60 kDa Ro/SSA and 52 kDa Ro/SSA.
Kurien BT, Chambers TL, Thomas PY, Frank MB, Scofield RH. Kurien BT, et al. Scand J Immunol. 2001 Mar;53(3):268-76. doi: 10.1046/j.1365-3083.2001.00870.x. Scand J Immunol. 2001. PMID: 11251884 Free article.
All patients with anti-Ro defined by precipitation bind a 60 000 Da antigen (60 kDa Ro), whereas some patients also bind a 52 000 Da molecule (52 kDa Ro). In general, antibody binding is directed against native 60 kDa Ro and denatured 52 kDa Ro. ...Thi …
All patients with anti-Ro defined by precipitation bind a 60 000 Da antigen (60 kDa Ro), whereas some patients also bind a 52 000 Da …
21-kDa polypeptide, a low-molecular-weight cyclophilin, is released from pollen of higher plants into the extracellular medium in vitro.
Yokota E, Ohmori T, Muto S, Shimmen T. Yokota E, et al. Planta. 2004 Apr;218(6):1008-18. doi: 10.1007/s00425-003-1177-2. Epub 2004 Jan 24. Planta. 2004. PMID: 14745555
In the case of C. japonica, however, it was released from pollen at alkaline pH above 8.5. The expression of 21-kDa polypeptide was not pollen-specific, because 21-kDa components immunoreactive with the anti-21-kDa polypeptide serum also existed in vegetative …
In the case of C. japonica, however, it was released from pollen at alkaline pH above 8.5. The expression of 21-kDa polypeptide was n …
A 130 kDa polypeptide immunologically related to the 180 kDa catalytic subunit of DNA polymerase alpha-primase complex is detected in early embryos of Drosophila.
Kuroda K, Ueda R. Kuroda K, et al. J Biochem. 1995 Apr;117(4):809-18. doi: 10.1093/oxfordjournals.jbchem.a124780. J Biochem. 1995. PMID: 7592543 Free article.
We detected the 180 kDa and the 72 kDa polypeptides in the extract prepared from a single Drosophila embryo by Western blotting, and a 130 kDa polypeptide immunologically related to the 180 kDa polypeptide was also detected in the extract. ...Even in u …
We detected the 180 kDa and the 72 kDa polypeptides in the extract prepared from a single Drosophila embryo by Western blottin …
Reversible association of a 97-kDa protein complex found at the tips of ciliary microtubules with in vitro assembled microtubules.
Wang W, Suprenant K, Dentler WL. Wang W, et al. J Biol Chem. 1993 Nov 25;268(33):24796-807. J Biol Chem. 1993. PMID: 8227041 Free article.
The 97-kDa protein-microtubule association can be disrupted by ATP and by adenosine 5'-O-(thio-triphosphate), and this ATP sensitivity requires a soluble factor in the crude 97-kDa protein fraction. ...These results suggest that the 97-kDa protein is part of …
The 97-kDa protein-microtubule association can be disrupted by ATP and by adenosine 5'-O-(thio-triphosphate), and this ATP sensitivit …
174,314 results
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