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1978 (1)
1Author    DhirendraL. NandiRequires 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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 TEI-XML for    default:Reihe_C/33/ZNC-1978-33c-0799_n.pdf 
 Identifier    ZNC-1978-33c-0799_n 
 Volume    33