| 2 | Author
| DhirendraL. Nandi | Requires cookie* | | Title
|  | | | Abstract
| The 14C labelled inactive protein obtained by sodium borohydride reduction of the enzyme, porphobilinogen syn thase of R h od op se u d om on a s sp h eroid es, in the presence of [4 -u C ] 5-aminolevulinic acid, gave on acid hydrolysis and subsequent electrophoresis or two-dimensional chromato graphy a m ajor radioactive spot which was confirmed to be N -f-[4-(-5am inovaleric acid) ] lysine (A L A -ly s in e) by comparing its co-chromatographic and electrophoretic be haviour with the chemically synthesized A L A -lysin e. A n e -N H , group of lysine residue of porphobilinogen synthase, is thus the binding site of the substrate, 5-aminolevulinic acid. | | |
Reference
| Z. Naturforsch. 33c, 799 (1978); received A p ril 25/June 6 1978 | | |
Published
| 1978 | | |
Keywords
| Borohydride Reduction, L abelled Protein, Hydrolysis Lysine, Active Site | | |
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| default:Reihe_C/33/ZNC-1978-33c-0799_n.pdf | | | Identifier
| ZNC-1978-33c-0799_n | | | Volume
| 33 | |
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