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Substance P synthesis by enzymatic fragment condensation using product–directed antibodies as molecular traps
Author(s) -
Nyberg Fred
Publication year - 1988
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.300010202
Subject(s) - chemistry , antibody , radioimmunoassay , enzyme , chromatography , substance p , endopeptidase , hydrolysis , condensation , stereochemistry , biochemistry , receptor , neuropeptide , physics , thermodynamics , immunology , biology
Abstract This paper describes the enzyme catalyzed synthesis of the undecapeptide substance P from its non‐associated fragments (1–7) and (8–11) or (1–8) and (9–11). The fragment condensation was mediated by the use of product specific antibodies as molecular traps. As catalyst a previously purified endopeptidase was used which specifically hydrolyzes substance P at the Phe 7 –Phe 8 and Phe 8 –Gly 9 bonds. The synthesis was performed in analytical scale and product formation was guided by reversed phase HPLC combined with radioimmunoassay. It appeared that the substance P fragments (1–8) and (9–11) were condensed to a larger extent than (1–7) and (8–11). This observation may well result from the higher affinity of the antibodies observed for substance P (8–11) as compared to that found for the other fragments. Increased concentration of the antibodies also seemed to result in enhanced resynthesis of substance P.