Primary structure of the porcine 89-kDa enamelin.
The primary structure of the 89-kDa enamelin found in porcine secretory enamel at an early stage of development was investigated. The fragments of the enamelin cDNA were amplified by polymerase chain-reaction from the first-strand enamelin cDNA, and were sequenced. The results indicated that the 89-kDa enamelin consisted of 627 amino acid residues and had a molecular mass of 70,448. A hydrophobic domain is located in the region of the 21st-62nd amino acid residues of the molecule. Acidic domains are located in two regions of the molecule-one in the region of the 135th-238th amino acid residues and the other in the C-terminal region. A basic domain is located in the region of the 239th-360th amino acid residues. The results also indicated that the low-molecular-weight enamelins were fragments derived from a prototype enamelin.
Fukae
M
M
Department of Biochemistry, School of Dental Medicine, Tsurumi University, Yokohama, Japan.
Tanabe
T
T
Murakami
C
C
Dohi
N
N
Uchida
T
T
Shimizu
M
M
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D018076:DNA, Complementary / Q000737:chemistry; D003746:Dental Enamel Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D017386:Sequence Homology, Amino Acid; D013552:Swine
D018076:DNA, Complementary; D003746:Dental Enamel Proteins; C038456:tuftelin