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Biomedical subjects

A C Wang

Publications and source records attributed to A C Wang.

At least 91 records · Page 5Linked to original sources
PubMed1980

Three M-components IgA lambda + IgG kappa n + IgG kappa h in one patient (DA): lack of shared idiotypic determinants between IgA and IgG, and the presence of an unusual kappa h chain of 30,000 M.W.

Two apparently homogeneous electrophoretic bands were found in the serum of a patient (DA) with multiple myeloma. These M-components were identified as IgA-lambda and IgG-kappa paraproteins bearing different idiotypic determinants. Further analysis of the L chains showed that the lambda-chain was homogeneous but the kappa-chain could be separated by SDS-polyacrylamide gel electrophoresis into two different bands. Both of them were associated with gamma-chains but one (termed kappa n) had normal m.w. (24,500) whereas the other (termed kappa h) was larger (m.w. 30,000). Sugar content of the two DA IgG, as determined by anthrone reaction, was similar in DA IgG kappa n (0.73%) and in DA IgG kappa h (1.1%), clearly demonstrating that the difference in m.w. was not due to a large sugar chain. Furthermore, the peptide map of the kappa h chain included nine peptides absent in those of four other control kappa-chains. Sequence analysis showed that the first 25 N-terminal amino acids of the kappa n differed from those of the kappa h chain at positions 4, 5, 15, 18, and 21. Thus the two kappa-chains had different framework regions.

Aged↗
PubMed1978

Hv(1), a variable-region genetic marker of human immunoglobulin heavy chains.

A new antigenic determinant was discovered with a hemagglutination-inhibition assay system. Designated Hv(1), it is located in the variable region of human immunoglobulin heavy chains of the G, M, and A classes. Pedigree and population analyses suggest that it has an autosomal dominant mode of inheritance. This represents the first description of an allotypic determinant in the variable region of human immunoglobulins.

Binding Sites, Antibody↗
PubMed1978

Monoclonal IgM cryoglobulinemia associated with gamma-3 heavy chain disease: immunochemical and biochemical studies.

A patient (Mia) with a monoclonal IgM(kappa) cryoglobulin (cryo IgM) developed additional heavy chain disease proteins of the gamma3 subclass 8 years later. Biochemical studies of the cryo IgM indicated that the heavy chain was VHI, but the NH2-terminal amino acid sequence of the light chain did not permit a definite assignment of its Vkappa subgroup. Two major fragments of the gamma3 chain were distinguishable by electrophoresis in sodium dodecyl sulfate polyacrylamide gel. The smaller component (designated Mia F) had a molecular weight of approximately 30 000 and the larger component (designated Mia S) 35 000. Both fragments had G3m(21) and G3m(27) allotypic determinants. These data and the NH2-terminal amino acid sequence of the gamma chain fragments suggested that Mia S consists of the major part of the gamma3 hinge region plus the CH2 and CH3 domains of the gamma3 chain, whereas Mia F may be derived from the former as a result of postsynthetic cleavage. The partial amino acid sequence of the Mia S fragment is homologous to the hinge region amino acid sequence of human gamma3 chains reported in the literature, with only one amino acid difference out of the 11 residues compared. This difference may represent an allotypic difference within the gamma3 subclass. Alternatively, the production of Mia S may have resulted from the accidental derepression of a "silent" constant region gene not expressed in normal individuals.

Amino Acid Sequence↗
PubMed1978

Immunoglobulin evolution: chemical study of clawed toad (Xenopus laevis) heavy and light chains.

NH2 terminal amino acid sequence determinations of clawed toad (Xenopus laevis) immunoglobulins indicate that approximately 30% of the heavy chains and less than 5% of the light chains have unblocked NH2 termini. The major amino acid sequence of the X. laevis 7S immunoglobulin heavy chains is the same as that of the 19S immunoglobulin heavy chains. Thus in the synthesis of the heavy chains, the VH genes coding for unblocked heavy chains can associate with CH genes of both the 19S and 7S classes. This association is particularly important in amphibians because, in contrast to mammals and birds, the majority of amphibian antibody-producing cells synthesize both 19S and 7S immunoglobulins and do not participate in the 'genetic switch' characteristic of lymphocyte differentiation in higher organisms. In X. laevis, the major amino acid sequence at the first twenty-four positions of the unblocked heavy chains shows approximately 54% difference from the prototype amino acid sequence of the mammalian VHIII subgroup. Thus, the VHIII gene(s) must have started to appear after the evolutionary divergence of the common ancestor of mammals and birds from the amphibian line. The amino acid composition of the X. Laevis 7S immunoglobulin heavy chains differs from that of its 19S immunoglobulins as well as those of human IgG and IgA. These data support the concepts (a) that amphibian 7S and 19S immunoglobins belong to distinct classes and (b) that amphibian 7S immunoglobulin does not resemble mammalian IgG or IgA.

Amino Acid Sequence↗
PubMed1977

Binding of E.coli lac repressor to non-operator DNA.

It is shown by melting profile analysis of lac repressor-DNA complexes that repressor binds tightly and preferentially (relative to single-stranded DNA) to double-stranded non-operator DNA. This binding stabilizes the DNA against melting and the repressor against thermal denaturation. Analysis of the extent of stabilization and the rate of dissociation of repressor from non-operator DNA as a function of sodium ion concentration shows, in confirmation of other studies,(3,4) that the binding constant (K(RD)) is very ionic strength dependent; K(RD) increases from approximately 10(6) M(-1) at approximately 0.1 M Na(+) to values in excess of 10(10) M(-1) at 0.002 M Na(+). Repressor bound to non-operator DNA is not further stabilized against thermal denaturation by inducer binding, indicating that the inducer and DNA binding sites probably represent separately stabilized local conformations. Transfer melting experiments are used to measure the rate of dissociation of repressor from operator DNA. These experiments show that most of the ionic strength dependence of the binding constant is in the dissociation process; the estimated dissociation rate constant decreases from greater than 10(-1) sec(-1) at [Na(+)] >/= 0.02 M to less than 10(-4) sec(-1) at [Na(+)] </= 0.002 M. Competition melting experiments are used to show that at 0.02 to 0.002 M Na(+) the affinity of lac repressor for various natural DNAs and synthetic double-stranded polynucleotides (including poly[d(m(6)A-T)], which carries a methyl group in the large groove) are approximately independent of base composition, except that the affinity of repressor for poly[d(A-T)] is approximately 2- to 3-fold greater than for the other DNAs tested. The affinity for single-stranded polynucleotides is atleast 50-fold less than for the doublehelical forms.

Bacterial Proteins↗
PubMed1976

Partial amino acid sequences of kappa-chains of rat immunoglobulins: genetic and evolutionary implications.

Partial amino acid sequences have been determined for several kappa-type light chains prepared from sera or urine of inbred LOU/C/Wsl rats bearing plasma cell tumors. Comparison of these sequences with those of human, rabbit, and mouse kappa-chains available in the literature indicates that the constant region of rat kappa-chains shows more amino acid sequence homology to that of the mouse kappa-chain than to human and rabbit kappa-chains, a result expected from the phylogenetic relationship of the species compared. Examination of the N-terminal amino acid sequences indicated that the variable regions of rat kappa-chains can also be classified into subgroups according to degree of sequence homology in a manner similar to that done for kappa-chains of other species (e.g., human, rabbit, and mouse). However, the prototype amino acid sequences of kappa-chain variable region subgroups of the rat were not homologous to those of other species including the closely related mouse. The implications of this observation with respect to the genetics and evolution of immunoglobulins are discussed.

Amino Acid Sequence↗
PubMed1976

Chemical and genetic characterization of a monoclonal IgA(lambda) protein with both cryo- and pyro-precipitability.

Studies of a monoclonal IgA (lambda) protein with both cryo- and pyro-precipitability show that it belongs to the IgA2 subclass and is positive for the A2m(2) allotypic marker. Like other cryoglobulins, this protein also has an unblocked light chain, and its heavy chain belongs to the VHI subgroup. The first 22 N-terminal amino acids of the lambda chain of this protein showed less than 65% homology with those of other human lambda chains but showed 86% identity with that of an amyloid fibril protein reported by others. The alpha chain of this protein appears to have more glutamic acid or glutamine, or both, and less isoleucine residues than other human alpha chains.

Amino Acid Sequence↗
PubMed1976

Heterogeneity of the protein moiety of carcinoembryonic antigens.

N-terminal amino acid sequences were determined for the protein moiety of carcinoembryonic antigen (CEA) isolated from three colon cancers that had metastasized to the liver. The results showed that the polypeptide portion of CEA preparations isolated from different tumors are not identical. Furthermore, each CEA preparation appeared to be heterogeneous within itself, since multiple amino acid residues were recovered at most of the positions following stepwise cleavage of the protein moiety of CEA molecules by automatic Edman degradation.

Amino Acid Sequence↗
PubMed1976

Immunological studies of human placentae: subclass and fragment specificity of binding of aggregated IgG by placental endothelial cells.

Fluorescein-conjugated heat-aggregated human IgG binds to endothelial cells of foetal stem vessels in cryostat sections of normal, full-term human placentae. No binding was observed using native human IgG of heat-aggregated human albumin, IgM or IgA2. No inhibition of binding of heat-aggregated human IgG was observed by pre-treatment of placental tissue sections with native IgG or non-aggregated Fc fragments. The binding was blocked using heat-aggregated Fc fragments prepared from IgG1, IgG2, IgG3 and IgG4 myeloma proteins, but not with heat-aggregated human light chains, Fab and F(ab)2 fragments of human IgG, or with heat-aggregated human IgM and IgA2. It is suggested that the placental endothelial cell receptor for aggregated IgG may function to keep immune complexes from entering the foetal circulation.

Antibody Specificity↗