Purification and Properties of Guanosine Triphosphate Cyclohydrolase and a Stimulating Protein from Comamonas Sp. (ATCC 11299a)
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference16 articles.
1. Biosynthesis of Pteridines and of Phenylalanine Hydroxylase Cofactor in Cell-free Extracts of Pseudomonas Species (ATCC 11299a)
2. Partial Purification and Properties of Guanosine Triphosphate Cyclohydrolase, the First Enzyme in Pteridine Biosynthesis, from Comamonas sp. (ATCC 11299a)
3. The Biosynthesis of Folic Acid
4. Identification of the Isomer of Dihydroneopterin Triphosphate Synthesized by Two Enzyme Fractions from Lactobacillus plantarum
5. Identification of d-erythro-Dihydroneopterin Triphosphate, the First Product of Pteridine Biosynthesis in Comamonas Sp. (ATCC 11299a)
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3. Rat GTP cyclohydrolase I is a homodecameric protein complex containing high-affinity calcium-binding sites 1 1Edited by W. Baumeister;Journal of Molecular Biology;1998-05
4. Pteridines. Part CVI. Isolation and characterization of limipterin (1-O-(L-erythro-biopterin-2?-yl)-?-N-acetylglucosamine) and its 5,6,7,8-tetrahydro derivative from green sulfur bacteriumChlorobium limicola f. thiosulfatophilum NCIB 8327;Helvetica Chimica Acta;1995-05-10
5. Partial Purification and Characterization of GTP Cyclohydrolase I from Spinach Leaves;Advances in Experimental Medicine and Biology;1993
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