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1978 (1)
1975 (1)
1Author    Jan AhlersRequires cookie*
 Title    Identification of Functional Croups of Pig Kidney Alkaline Phosphatase by Specific Inhibitors  
 Abstract    Inactivation studies with 17 group-specific inhibitors showed that amino, hystidyl and tyrosyl residues probably are components of the active and/or regulatory sites of pig kidney alkaline phosphatase. 
  Reference    (Z. Naturforsch. 30c, 829 [1975]; received July 17/September 19 1975) 
  Published    1975 
  Keywords    Pig Kidney Alkaline Phosphatase, Active Site, Inactivation Studies, Group-Specific Inhibitors 
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 TEI-XML for    default:Reihe_C/30/ZNC-1975-30c-0829_n.pdf 
 Identifier    ZNC-1975-30c-0829_n 
 Volume    30 
2Author    DhirendraL. NandiRequires cookie*
 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