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1994 | 1 |
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Electrostatic channeling of oxaloacetate in a fusion protein of porcine citrate synthase and porcine mitochondrial malate dehydrogenase.
Biochemistry. 1999 Jan 19;38(3):881-9. doi: 10.1021/bi982195h.
Biochemistry. 1999.
PMID: 9893982
Mitochondrial malate dehydrogenase and citrate synthase are sequential enzymes in the Krebs tricarboxylic acid cycle. We have shown [Lindbladh, C., Rault, M., Hagglund, C., Small, W. C., Mosbach, K., Bulow, L., Evans, C., and Srere, P.A (1994) Biochemistry 33, 11692 …
Mitochondrial malate dehydrogenase and citrate synthase are sequential enzymes in the Krebs tricarboxylic acid cycle. We have shown [Lind …
Preparation and kinetic characterization of a fusion protein of yeast mitochondrial citrate synthase and malate dehydrogenase.
Lindbladh C, Rault M, Hagglund C, Small WC, Mosbach K, Bülow L, Evans C, Srere PA.
Lindbladh C, et al.
Biochemistry. 1994 Oct 4;33(39):11692-8. doi: 10.1021/bi00205a004.
Biochemistry. 1994.
PMID: 7918385
The fusion protein produced was isolated and purified. Gel filtration studies indicated that CS1/MDH1 had a M(r) of approximately 170,000. Western blotting analysis with SDS gel indicated a M(r) of approximately 90,000-95,000 (theoretical M(r) = 87,000). This …
The fusion protein produced was isolated and purified. Gel filtration studies indicated that CS1/MDH1 had a M(r) of approximately 170 …
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Selection of a cyclic nonapeptide inhibitor to alpha-chymotrypsin using a phage display peptide library.
Krook M, Lindbladh C, Eriksen JA, Mosbach K.
Krook M, et al.
Mol Divers. 1997-1998;3(3):149-59. doi: 10.1023/a:1009697515328.
Mol Divers. 1997.
PMID: 9680646
The inhibition constant for alpha-chymotrypsin was estimated to be 10(-6) M. Phage clones expressing this peptide had a lower affinity for phenylmethylsulfonylfluoride-modified alpha-chymotrypsin than for natural alpha-chymotrypsin as determined by an enzyme immunosorbent …
The inhibition constant for alpha-chymotrypsin was estimated to be 10(-6) M. Phage clones expressing this peptide had a lower affinit …
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