High impact information on TUFT1

• Of the remaining very small amounts of non-serum or salivary protein isolated from the enamelin extracts, three minor components were isolated which had N-terminal amino acid sequences which were not similar to any known protein in the protein sequence data base and could therefore conceivably be true 'enamelins' synthesized by ameloblasts [1].
• On the basis of the data presented, studies employing antibodies to the so-called enamelin proteins and hypotheses as to their molecular conformation, their roles as evolutionary markers, or their positive role in mineralization should be reconsidered and reviewed [1].
• The major enamelin protein component present in EDTA or EDTA/guanidine hydrochloride extracts of developing bovine enamel has a molecular mass of about 67 kDa; it has an amino acid composition similar to that of bovine serum albumin and reacts with polyclonal and monoclonal antibodies to albumin [1].
• The serum proteins alpha-2 HS glycoprotein, gamma-globulin and fetuin, and the proline-rich salivary protein termed P-B were also identified in the enamelin extract [1].
• The bovine tuftelin gene was cloned and its structure determined by DNA sequence analysis and comparison to that of bovine tuftelin cDNA [2].

Analytical, diagnostic and therapeutic context of TUFT1

• Molecular cloning and characterization of the bovine tuftelin gene [2].
• Affinity chromatography of "Enamelin Extracts" of developing bovine molar enamel on CNBr activated Sepharose 4B to which polyclonal antibodies of whole bovine serum and fetuin were cross-linked, revealed that at most, only 1-2% of the proteins in the extracts were not bound to the columns [3].

References