Primary Structure of the Porcine 89-kDa Enamelin

Author:

Fukae M.1,Tanabe T.1,Murakami C.2,Dohi N.2,Uchida T.2,Shimizu M.1

Affiliation:

1. Department of Biochemistry School of Dental Medicine Tsurumi University Tsurumi-ku. Yokohama 230, Japan

2. Department of Oral Anatomy School of Dentistry Hiroshima University Minami-ku, Hiroshima 734, Japan

Abstract

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 21 st-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.

Publisher

SAGE Publications

Subject

General Medicine

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