01995nas a2200373   4500000000100000008004100001260001300042653002400055653001200079653002600091653002700117653002400144653002300168653002900191653002300220653001400243653001100257653001200268653002800280653002100308653004800329653002500377653001200402653003400414100001800448700001300466700001300479700001700492245013400509300001000643490000700653520094700660022001401607       1995                            d  c1995 Jun10aAmino Acid Sequence10aAnimals10aAntibodies, Bacterial10aAntibodies, Monoclonal10aAntigens, Bacterial10aBacterial Proteins10aChromatography, Affinity10aCytochrome b Group10aFerritins10aHumans10aleprosy10aMolecular Sequence Data10aMolecular Weight10aMycobacterium avium subsp. paratuberculosis10aMycobacterium leprae10aRabbits10aSequence Homology, Amino Acid1 aDeshpande R G1 aKhan M B1 aBhat D A1 aNavalkar R G00aImmunoaffinity chromatographic isolation of a high molecular weight seroreactive protein from Mycobacterium leprae cell sonicate.  a163-90 v113 a<p>The purpose of this study was to isolate Mycobacterium leprae antigen(s) by immunoaffinity chromatography using immunoglobulins from leprosy patients and from rabbit anti-M. leprae hyperimmune serum coupled to CNBr-Sepharose 4B. A high molecular weight (M(r)) M. leprae protein (MLP) with a subunit M(r) of 22,000 was isolated. MLP was recognized by monoclonal antibody MMPII1G4 which is known to react with MMPII, a 22 kDa protein of M. leprae. The N-terminal sequence of the 22 kDa subunit (Met-gln-gly-asp-pro-asp-val-leu-arg-leu-leu-asn-glu-gln-leu-thr) was identical to MMPII and to antigen D (bacterioferritin) of M. paratuberculosis. It showed 44% homology with N-terminal end of E. coli bacterioferritin. In ELISA, MLP showed 100% and 60% positivity with leprosy and TB sera respectively as compared to normal healthy sera. The role of bacterioferritin in M. leprae and the importance of MLP as an immunogen has been discussed.</p>  a0928-8244