RESUMO
The common regions of two lambda chains (amino acid residues 109 to 213) have been partially sequenced. These two human immunoglobulin chains have lysine at position 190, but are otherwise identical in their common-region sequence to four reported lambda chains that have arginine at position 190. The single amino acid interchange at position 190 may be explained either by an ambiguous codon at this position or by a gene duplication so recent that only a single mutational event has occured.
Assuntos
Sequência de Aminoácidos , Peptídeos/análise , gama-Globulinas/análise , Arginina , Proteína de Bence Jones/análise , Humanos , Lisina , Biologia Molecular , MutaçãoRESUMO
Two antigenic subtypes of human lambda polypeptide chains were distinguished by rabbit antiserum produced to a lambda Bence Jones protein. Lambda Bence Jones proteins and G myeloma proteins with lambda light chains were identified as being in one or the other subtype. The Oz (+) lambda chain subtype is present in light chains from pooled normal human immunoglobulin G and in whole normal immunoglobulin G molecules.
Assuntos
Proteína de Bence Jones , Peptídeos/análise , gama-Globulinas/análise , Animais , Humanos , Soros Imunes , Imunodifusão , CoelhosRESUMO
"Amyloid" fibrils have been created from some human Bence Jones proteins by proteolytic digestion under physiologic conditions. These fibrils with an antiparallel, beta-pleated sheet conformation consist of only a portion of the variable region of the immunoglobulin light polypeptide chain and share the physical properties of amyloid fibrils. The relation between amyloidosis and immunoglobulins is thus more firmly established and a pathogenetic mechanism for amyloid fibril formation is suggested.
Assuntos
Amiloide/biossíntese , Proteína de Bence Jones/metabolismo , Sequência de Aminoácidos , Amiloide/análise , Humanos , Concentração de Íons de Hidrogênio , Técnicas In Vitro , Microscopia Eletrônica , Peptídeo Hidrolases , Temperatura , Difração de Raios XRESUMO
A new heavy chain disease protein ((gamma)HCD-JM) has been characterized by antigenic and structural criteria. The protein belongs to the IgG3-subclass and is closely related to Fc-fragment of G3-immunoglobulins. The predominant N-terminal amino acid of this protein is glutamic acid in the uncyclized form, and that of another (gamma)HCD is glycine. Studies of the N-terminal peptides indicate that the N-terminal portion of the (gamma)3-heavy polypeptide chain is absent from the (gamma)HCD-JM. These findings rule out a process of normal heavy chain initiation and a large deletion of the Fd region as being responsible for these two heavy chain disease proteins. The (gamma)HCD-JM is a secretory product of cells from bone marrow as shown by studies of in vitro incorporation of amino acids-(14)C. Bone marrow and lymph node have a population of lymphoplasmacytic cells which by immunofluorescence contain (gamma)-heavy chain antigens in the absence of light chain antigens.