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M

M. Shimizu

Researcher at Tsurumi University

Publications -  21
Citations -  2157

M. Shimizu is an academic researcher from Tsurumi University. The author has contributed to research in topics: Enamel paint & Amelogenin. The author has an hindex of 20, co-authored 21 publications receiving 2112 citations.

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Resolution-enhanced Fourier transform infrared spectroscopy study of the environment of phosphate ion in the early deposits of a solid phase of calcium phosphate in bone and enamel and their evolution with age: 2. Investigations in the nu3PO4 domain.

TL;DR: Comparison of the FTIR spectra of biological apatites with those of synthetic, nonapatitic-containing phosphate minerals shows that the presence of these bands does not arise from nonapAtitic, well-defined phases; they are due to the local environment of phosphate ions which may possibly be loosely related or perhaps unrelated to the phosphate groups present in the well-crystallized nonap atitic calcium phosphates.
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A resolution-enhanced Fourier transform infrared spectroscopic study of the environment of the CO3(2-) ion in the mineral phase of enamel during its formation and maturation.

TL;DR: A comparison of the parameters assessing the degree of crystallinity of the mineral phase from υ2CO32− and υ4PO32− infrared absorption data reveals a significant discrepancy related to the nonhomogeneous partition of the CO32− ion in the Mineral phase.
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Selective adsorption of porcine-amelogenins onto hydroxyapatite and their inhibitory activity on hydroxyapatite growth in supersaturated solutions

TL;DR: The results suggest that the originally secreted amelogenin 2a may play an active role in amelogenesis, and that enamel mineralization could be regulated by the secretion of amelgenins and their inactivation through partial enzymic degradation, prior to their complete removal.
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Sheathlin: Cloning, cDNA/Polypeptide Sequences, and Immunolocalization of Porcine Enamel Sheath Proteins

TL;DR: It is proposed that the porcine sheath proteins and their proteolytic cleavage products be designated "sheathlin", and the protein encoded by the sheathlin cDNA is preferentially localized in theSheath space.
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Purification, characterization and cloning of enamel matrix serine proteinase 1

TL;DR: To isolate and characterize cDNA clones encoding this proteinase, two degenerate primer approaches were used to amplify part of the coding region using polymerase chain-reaction (PCR) and yielded PCR amplification products that served as probes for screening a porcine enamel organ epithelia-specific cDNA library.