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Biomedical subjects

J B Adlersberg

Publications and source records attributed to J B Adlersberg.

6 recordsLinked to original sources
PubMed1982

Isolation and biochemical characterization of the tryptic fragments of bovine nasal-cartilage proteoglycan monomer of high buoyant density.

Relatively homogeneous fractions of proteoglycan fragments were prepared from tryptic digests of the 4M-guanidinium chloride extract of bovine nasal cartilage. Glycosaminoglycan-containing fragments were separated from non-proteoglycan contaminants by ion-exchange chromatography and fractionated by equilibrium density-gradient centrifugation under dissociative conditions. The fractions of highest buoyant density were chromatographed on a column of Sepharose 4B, digested with chondroitinase ABC and chromatographed on a column of Sepharose 6B, yielding two distinct fractions: fraction B/6B-4 contained fragments from the chondroitin sulphate-bearing region of the proteoglycan monomer, and fraction B/6B-2 fragments from the keratan sulphate-rich region, most probably including a chondroitin sulphate-bearing monomer segment. By dansyl chloride analysis, fraction B/6B-2 had alanine and leucine as sole and fraction B/6B-4 had isoleucine and leucine as greatly predominant N-terminal amino acids, indicative of the relative homogeneity of these preparations of cartilage proteoglycan monomer fragments.

Amino Acids↗
PubMed1978

An unusual case of a plasma cell neoplasm with an IgG3lambda myeloma and a gamma3 heavy chain disease protein.

A unique case of gamma3 heavy chain disease with two related serum proteins is reported. One molecule appears to be an IgG3lambda myeloma protein. The second molecule is a dimer of a shortened gamma3 heavy chain that has an unblocked amino terminus and lacks the VH and CH1 domains. Its probable origin as a synthetic product is discussed. The clinical and pathologic features of this patient resemble those of other patients with gamma heavy chain disease more than those of patients with multiple myeloma. It seems likely that the heavy chain disease protein is the result of a mutational event in the malignant clone originally producing the myeloma protein.

Centrifugation, Density Gradient↗
PubMed1975

Repetitive hinge region sequences in human IgG3: isolation of an 11,000-dalton fragment.

The heavy chain (gamma-3) of the IgG3 subclass of human immunoglobulins has a molecular weight of 60,000, instead of the 50,000 value reported for gamma-1, gamma-2, and gamma-4 heavy chains. By use of protein Omm, a gamma-3 heavy chain disease protein, it was possible to isolate and analyze the extra fragment. Protein Omm had a molecular weight of 40,000, glycine as its sole NH-2-terminal, and contained only the hingee region and the C-H-2 and C-H-3 domains. CNBr cleavage at Met 252 (gamma-1 numbering) yielded the hinge fraction (Fh fragment). On the basis of the molecular weight of Fh (11,000), its amino-acid composition, its partial sequence, and its unexpectedly low number of tryptic peptides, it is postulated that the extra fragment in gamma-3 heavy chains represents a series of similar or identical duplications of sections of the previously reported gamma-3 hinge region. In addition, there are striking homologies with the hinge region of alpha-1 and alpha-2 heavy chains, one of which also has duplications. The relationship of these hinge structures in different immunoglobulins supports the concept that this region is coded by a unique, small piece of DNA, which has evolved in parallel manner with the immunogolbulin genes by partial duplications and/or crossingover.

Amino Acid Sequence↗
PubMedDate not supplied

The immunoglobulin hinge (interdomain) region.

The hinge region is a flexible amino acid stretch in the central part of the heavy chains of the IgG and IgA immunoglobulin classes, which links these 2 chains by disulfide bonds. It is rich in cysteine and proline amino acids, extremely variable in amino acid sequence, and has no resemblance to any other immunoglobulin region. The hinges in these 2 classes are compared and contrasted. Such a distinct molecular structure does not exist around the inter-heavy disulfide bonds of the other Ig classes, but a portion of the IgM heavy chain has similar properties to the gamma hinge. This similarity suggests one hypothesis for the genetic origin of the hinge region; data supporting 2 other hypotheses are also presented.

Amino Acid Sequence↗