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Biomedical subjects

K Titani

Publications and source records attributed to K Titani.

285 records · Page 16Linked to original sources
PubMed1967

Evolution of immunoglobulins: structural homology of kappa and lambda Bence Jones proteins.

The amino acid sequence of a human lamba chain has been determined. There are many identities in sequence with human kappa chains, but this intraspecies homology is less than the interspecies homology of kappa light chains of man and mouse. Structural relationships suggest a common evolutionary origin and early differentiation of light- and heavy-chain genes.

Amino Acid Sequence↗
PubMed1966

Immunoglobulin structure: variation in the sequence of Bence Jones proteins.

Analysis of the amino acid sequence of one Bence Jones protein is almost comtplete. Many points of interchange occur in the amino terminal. portion of the molecule relative to partial-sequence data for other proteins. Most, but not all, are, compartible with one-step mutations. Such structural variation in immunoglobulin light chains may result from many related genes.

Amino Acid Sequence↗
PubMed1965

Immunoglobulin structure: partial amino acid sequence of a Bence Jones protein.

Sequence analysis and ordering of the soluble tryptic peptides of one Bence Jones protein and comparison with partial sequence data for another have revealed many structural differences in the half of the molecule with the terminal amino group, but only one structural difference in the half of the molecule having the terminal carboxyl group. Somatic chromosomal rearrangements may effect such changes and account for variability in antibody structure.

Amino Acid Sequence↗
PubMedDate not supplied

Hyperphosphorylation of tau in PHF.

Tau in PHF is known to be highly phosphorylated and immunochemical study has indicated the similarity of the phosphorylation between PHF-tau and fetal tau. We have determined the exact phosphorylation sites in both PHF-tau and fetal rat tau by ion-spray mass spectrometry and sequencing of ethanethiol-modified peptides. In PHF-tau, 19 sites have been identified; all the phosphorylation sites except for Ser-262 are localized to the amino- and carboxyl-terminal flanking regions of the microtubule-binding domain. Half of them are shared by fetal tau. Thus, PHF-tau is much more phosphorylated. Whereas most of the sites in fetal tau are proline-directed, half of them in PHF-tau are nonproline-directed. Overall, the hyperphosphorylation of PHF-tau can be considered to consist of fetal-type phosphorylation and additional proline-directed and nonproline-directed phosphorylation. This extraphosphorylation may provide PHF-tau with the unusual characteristics including assembly incompetence.

Aged↗