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Relative molecular mass determination of a major, highest relative molecular mass extracellular amelogenin of developing bovine enamel
Author(s) -
Strawich E.,
Poon P.M.,
Renugopalakrishnan V.,
Glimcher M.J.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80604-9
Subject(s) - amelogenin , molecular mass , chemistry , chromatography , ultracentrifuge , enamel paint , sedimentation equilibrium , high performance liquid chromatography , biochemistry , enzyme , gene , medicine , dentistry
Proteins of developing bovine enamel were fractionated by molecular sieving and ion‐exchange chromatography. The major fraction corresponding to the highest M r amelogenin of M r ~26000–30000 was isolated and its M r determined by SDS‐PAGE, molecular sieving on G‐100 resin and high performance liquid chromatography and by sedimentation‐equilibrium ultracentrifugation, the latter three procedures in guanidine hydrochloride. SDS‐PAGE and HPLC molecular sieving, employing commonly used M r standards, gave M r values of ~22000–26000. SDS‐PAGE and HPLC molecular sieving, using proline‐rich CNBr peptides of collagen as standards, and sedimentation‐equilibrium ultracentrifugation, gave M r values of ~15000–18000 and ~17385, respectively. These latter values correspond well with those reported earlier and with the M r of the major amelogenin computed from recent amino acid sequence data (~19000). It is concluded that the recently described, highest M r amelogenin of M r = 26000–30000 is not a new component but is identical to the proline‐rich components having relative molecular masses ranging from 15000 to 18000 described much earlier by several groups of workers.