Tritsch D - Search Results

1

Evidence for the presence of anion-recognition sites in pig-liver aldehyde reductase. Modification by phenyl glyoxal and p-carboxyphenyl glyoxal of an arginyl residue located close to the substrate-binding site.

Branlant G, Tritsch D, Biellmann JF. Branlant G, et al. Among authors: tritsch d. Eur J Biochem. 1981 Jun 1;116(3):505-12. doi: 10.1111/j.1432-1033.1981.tb05365.x. Eur J Biochem. 1981. PMID: 7021149 Free article. No abstract available.

2

4-Chloroacetylpyridine adenine dinucleotide. A highly reactive and chromophoric affinity label of glyceraldehyde-3-phosphate dehydrogenase from sturgeon.

Tritsch D, Eiler-Samama B, Svircevic J, Albrecht AM, Branlant G, Biellmann JF. Tritsch D, et al. Eur J Biochem. 1989 Apr 15;181(1):215-22. doi: 10.1111/j.1432-1033.1989.tb14713.x. Eur J Biochem. 1989. PMID: 2714279 Free article.

3

Properties of the charge-transfer transition observed in glyceraldehyde-3-phosphate dehydrogenase from sturgeon muscle alkylated by 3-chloroacetylpyridine--adenine dinucleotide. Characterisation of the modified amino acid.

Branlant G, Tritsch D, Eiler B, Wallen L, Biellmann JF. Branlant G, et al. Among authors: tritsch d. Eur J Biochem. 1982 Dec 15;129(2):437-46. doi: 10.1111/j.1432-1033.1982.tb07069.x. Eur J Biochem. 1982. PMID: 7151807 Free article.

4

Study of non-covalent enzyme-inhibitor complexes of aldose reductase by electrospray mass spectrometry.

Potier N, Barth P, Tritsch D, Biellmann JF, Van Dorsselaer A. Potier N, et al. Among authors: tritsch d. Eur J Biochem. 1997 Jan 15;243(1-2):274-82. doi: 10.1111/j.1432-1033.1997.0274a.x. Eur J Biochem. 1997. PMID: 9030749 Free article.

5

X-ray analysis of D-xylose isomerase at 1.9 A: native enzyme in complex with substrate and with a mechanism-designed inactivator.

Carrell HL, Glusker JP, Burger V, Manfre F, Tritsch D, Biellmann JF. Carrell HL, et al. Among authors: tritsch d. Proc Natl Acad Sci U S A. 1989 Jun;86(12):4440-4. doi: 10.1073/pnas.86.12.4440. Proc Natl Acad Sci U S A. 1989. PMID: 2734296 Free PMC article.

6

Mechanism-based inhibition of proline dehydrogenase by proline analogues.

Tritsch D, Mawlawi H, Biellmann JF. Tritsch D, et al. Biochim Biophys Acta. 1993 Sep 3;1202(1):77-81. doi: 10.1016/0167-4838(93)90065-y. Biochim Biophys Acta. 1993. PMID: 8373828

7

Study of non-covalent enzyme-inhibitor complexes of aldose reductase by electrospray mass spectrometry.

Potier N, Barth P, Tritsch D, Biellmann JF, Van Dorsselaer A. Potier N, et al. Among authors: tritsch d. Adv Exp Med Biol. 1997;414:453-4. doi: 10.1007/978-1-4615-5871-2_51. Adv Exp Med Biol. 1997. PMID: 9059650 No abstract available.

8

Mass spectrometry as a novel approach to probe cooperativity in multimeric enzymatic systems.

Rogniaux H, Sanglier S, Strupat K, Azza S, Roitel O, Ball V, Tritsch D, Branlant G, Van Dorsselaer A. Rogniaux H, et al. Among authors: tritsch d. Anal Biochem. 2001 Apr 1;291(1):48-61. doi: 10.1006/abio.2000.4975. Anal Biochem. 2001. PMID: 11262155

9

[Change of cholesterol oxidase of Brevibacterium sterolicum and substrate specificity].

Loubat-Hugel C, Tritsch D, Biellmann JF. Loubat-Hugel C, et al. Among authors: tritsch d. C R Acad Sci III. 1994 Apr;317(4):299-303. C R Acad Sci III. 1994. PMID: 8000910 French.

10

3'-Beta-ethynyl and 2'-deoxy-3'-beta-ethynyl adenosines: first 3'-beta-branched-adenosines substrates of adenosine deaminase.

Tritsch D, Jung PM, Burger A, Biellmann JF. Tritsch D, et al. Bioorg Med Chem Lett. 2000 Jan 17;10(2):139-41. doi: 10.1016/s0960-894x(99)00639-3. Bioorg Med Chem Lett. 2000. PMID: 10673097

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