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W D Baldwin

Publications and source records attributed to W D Baldwin.

3 recordsLinked to original sources

Human transferrin: cDNA characterization and chromosomal localization.

Transferrin (Tf) is the major iron binding protein in vertebrate serum. It shares homologous amino acid sequences with four other proteins: lactotransferrin, ovotransferrin, melanoma antigen p97, and HuBlym-1. Antigen p97 and the Tf receptor genes have been mapped on human chromosome 3. The goal of the study described here was to initiate the characterization of the Tf gene by identifying and characterizing its cDNA and mapping its chromosomal location. Recombinant plasmids containing human cDNA encoding Tf have been isolated by screening an adult human liver library with a mixed oligonucleotide probe. Within the 2.3 kilobase pairs of Tf cDNA analyzed, there is a probable leader sequence encoded by 57 nucleotides followed by 2037 nucleotides that encode the homologous amino and carboxyl domains. During evolution, three areas of the homologous amino and carboxyl domains have been strongly conserved, possibly reflecting functional constraints associated with iron binding. Chromosomal mapping by in situ hybridization and somatic cell hybrid analysis indicate that the Tf gene is located at q21-25 on human chromosome 3, consistent with linkage of the Tf, Tf receptor, and melanoma p97 loci.

Amino Acid Sequence↗

Identification and characterization of human haptoglobin cDNA.

Recombinant plasmids containing human cDNA encoding haptoglobin, a plasma protein that binds free hemoglobin, have been isolated by screening an adult human liver library with a mixed oligonucleotide probe. Four cDNA clones containing inserts have been obtained that span 1,218 nucleotides of the haptoglobin coding sequence, including the 3' end of the haptoglobin cDNA. The cDNA sequence included a leader sequence followed by alpha 2-chain and beta-chain sequences. A heretofore unseen arginine residue was deduced between the human alpha- and beta-chain sequences. This is a probable site of limited proteolysis leading to the formation of the alpha and beta polypeptides in mature haptoglobin. A comparison of the haptoglobin alpha-beta-junction region and the heavy-light-chain junction of tissue-type plasminogen activator strengthens the evolutionary homology found in haptoglobin and the serine proteases. The Hp alpha 2 gene, which was shown earlier to be a partial duplication produced by unequal crossing-over between Hp alpha 1 genes, has been impossible to align by protein characterization. The cDNA sequence establishes the alignment of Hp alpha 2FS in the Hp alpha 2 gene studied here.

Amino Acid Sequence↗