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At least 613 records · Page 34Linked to original sources
PubMed1994

Cross-reactions of anti-immunoglobulin sera with synthetic T-cell receptor beta peptides: mapping on a 3-dimension model.

The derived amino acid sequences of human T-cell receptor beta chain shows significant homology to lambda light chains of immunoglobulins in its variable, joining, and constant regions. We assessed the cross-reactivity between Tcr beta chains and immunoglobulin light chains by determining the capacity of rabbit antisera to human or murine immunoglobulins to react to a synthesized set of nested, overlapping 16-mer peptides corresponding to the VDJC sequence of the Tcr beta chain YT35. The observed reactivities were consistent with homologies to lambda and kappa light chains, the strongest reactivity being with a peptide that corresponds to the "switch peptide" of light chains, as assessed by ELISA binding and competitive inhibitions assays. Other regions reactive with anti-light chain sera corresponded to CDR1 and Fr3 segments of the variable domain and a segment of the constant region predicted to loop out of the tight globular structure. The peptide immunochemical results, together with the identification of specific regions of sequence correspondence between Tcr beta and the characterized lambda light chain Mcg, allowed us to develop a 3-dimensional model of the beta chain consistent with its role in antigen recognition.

Animals↗
PubMed1986

Structure of the hepatitis A virion: peptide mapping of the capsid region.

Milligram amounts of highly purified hepatitis A virus (HAV) were obtained from persistently infected cell cultures. The HAV polypeptides were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and transferred to nitrocellulose for detection by an enzyme-linked immunotransfer blot procedure. The HAV nucleotide-derived amino acid sequence was subjected to computer analysis to identify potential immunogenic regions within the HAV capsid polypeptides. Synthetic peptides corresponding to selected regions of each of the larger putative capsid polypeptides were coupled to keyhole limpet hemocyanin and used to immunize rabbits. Four of six anti-HAV peptide sera were strongly reactive. Antipeptide serum generated against amino acids (a.a.) 75 through 82 reacted with the 27,000-molecular-weight (MW) polypeptide; serum against a.a. 279 through 285 reacted with the 29,000-MW HAV polypeptide; and sera against a.a. 591 through 602 and 606 through 618 reacted with the 33,000-MW HAV polypeptide. These reactions enabled the identification of the gene order of the larger HAV P1 region gene products. Our data indicate the following molecular weights: HAV VP2 or 1B, 27,000; HAV VP3 or 1C, 29,000; and HAV VP1 or 1D, 33,000.

Amino Acid Sequence↗
PubMed1978

Peptide mapping characterization of viral proteins generated in a cell-free coupled system for the transcription and translation of influenza virus mRNA.

In a coupled cell-free system for the transcription and translation of the influenza mRNA's, containing detergent-disrupted purified NWS influenza virion and a micrococcal nuclease-preincubated rabbit reticulocyte lysate, five unglycosylated viral proteins (NS1, M, NP, P1, and P3) were easily produced and isolated. Their identification was based on the electrophoretic separation of peptide fragments resulting from their partial digestion with proteases of restricted specificity (D.W. Cleveland, S. G. Fisher, N. W. Kirschner, and U. K. Laemmli, J. Biol. Chem. 252:1102-1106, 1977).

Cell-Free System↗
PubMed1985

Similarity of pituitary and pineal human oxytocin neurophysins indicated by peptide mapping after radioactive alkylation and proteolysis.

We have compared the immunoreactive oxytocin neurophysin from the human pineal gland with human neurohypophyseal neurophysin. The two proteins were reduced and carboxymethylated with [14C]-iodoacetic acid. Since the pineal protein was available only in a very small amount, we were obliged to use [12C]-carboxymethyl apomyoglobin as a nonalkylatable carrier. The trypsin and subtilisin digests of the two labelled proteins were compared by high-voltage electrophoresis on paper, partition paper chromatography, and high-performance liquid chromatography. The distribution of radioactivity in the above peptide separations suggests a great similarity between the two proteins and few significant differences. As far as we are aware, this study is the first attempt to analyze an extrahypophyseal neurophysin at the molecular level.

Alkylation↗