Complete amino acid sequence of amelogenin in developing bovine enamel

Pure amelogenin protein in developing bovine incisor enamel was isolated and its primary structure was investigated by sequencing the peptides obtained after clostripain and chymotrypsin digestions and CNBr degradation with an automated Edman sequencer. The enamel protein was found to be composed of...

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Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 121; no. 2; pp. 592 - 597
Main Authors Takagi, Tohru, Suzuki, Michiko, Baba, Tomomi, Minegishi, Kyomi, Sasaki, Satoshi
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.01.1984
Subjects
Amelogenin
Amino Acid Sequence
Animals
Cattle
Chemical Phenomena
Chemistry
dental enamel
Dental Enamel - growth & development
Dental Enamel - metabolism
Dental Enamel Proteins - isolation & purification
incisors
Molecular Weight
Peptide Fragments - isolation & purification
Phosphates - isolation & purification
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Summary:Pure amelogenin protein in developing bovine incisor enamel was isolated and its primary structure was investigated by sequencing the peptides obtained after clostripain and chymotrypsin digestions and CNBr degradation with an automated Edman sequencer. The enamel protein was found to be composed of 170 amino acid residues with one phosphate having a molecular weight of 19,350 and its complete amino acid sequence was elucidated. This protein has no sequence homology with any other tissue or secretory protein of known structure.
Bibliography:L
L50
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ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(84)90223-7