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Osteonectin cDNA Sequence Reveals Potential Binding Regions for Calcium and Hydroxyapatite and Shows Homologies with Both a Basement Membrane Protein (SPARC) and a Serine Proteinase Inhibitor (Ovomucoid)
by
Bolander, Mark E.
, Fisher, Larry W.
, Yamada, Yoshihiko
, Young, Marian F.
, Termine, John D.
in
Amino Acid Sequence
/ Amino acids
/ Analytical, structural and metabolic biochemistry
/ Animals
/ Base Sequence
/ Biochemistry
/ Biological and medical sciences
/ Bones
/ Calcium
/ Calcium - metabolism
/ Carrier Proteins - genetics
/ Carrier Proteins - metabolism
/ Cattle
/ Complementary DNA
/ DNA - analysis
/ Durapatite
/ Egg Proteins - metabolism
/ Fundamental and applied biological sciences. Psychology
/ Generally accepted auditing standards
/ Hydroxyapatites - metabolism
/ Miscellaneous
/ Molecular Sequence Data
/ Osteonectin
/ Ovomucin - metabolism
/ Proteins
/ Sequencing
/ Serine Proteinase Inhibitors
/ Ungulates
1988
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Osteonectin cDNA Sequence Reveals Potential Binding Regions for Calcium and Hydroxyapatite and Shows Homologies with Both a Basement Membrane Protein (SPARC) and a Serine Proteinase Inhibitor (Ovomucoid)
by
Bolander, Mark E.
, Fisher, Larry W.
, Yamada, Yoshihiko
, Young, Marian F.
, Termine, John D.
in
Amino Acid Sequence
/ Amino acids
/ Analytical, structural and metabolic biochemistry
/ Animals
/ Base Sequence
/ Biochemistry
/ Biological and medical sciences
/ Bones
/ Calcium
/ Calcium - metabolism
/ Carrier Proteins - genetics
/ Carrier Proteins - metabolism
/ Cattle
/ Complementary DNA
/ DNA - analysis
/ Durapatite
/ Egg Proteins - metabolism
/ Fundamental and applied biological sciences. Psychology
/ Generally accepted auditing standards
/ Hydroxyapatites - metabolism
/ Miscellaneous
/ Molecular Sequence Data
/ Osteonectin
/ Ovomucin - metabolism
/ Proteins
/ Sequencing
/ Serine Proteinase Inhibitors
/ Ungulates
1988
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Osteonectin cDNA Sequence Reveals Potential Binding Regions for Calcium and Hydroxyapatite and Shows Homologies with Both a Basement Membrane Protein (SPARC) and a Serine Proteinase Inhibitor (Ovomucoid)
by
Bolander, Mark E.
, Fisher, Larry W.
, Yamada, Yoshihiko
, Young, Marian F.
, Termine, John D.
in
Amino Acid Sequence
/ Amino acids
/ Analytical, structural and metabolic biochemistry
/ Animals
/ Base Sequence
/ Biochemistry
/ Biological and medical sciences
/ Bones
/ Calcium
/ Calcium - metabolism
/ Carrier Proteins - genetics
/ Carrier Proteins - metabolism
/ Cattle
/ Complementary DNA
/ DNA - analysis
/ Durapatite
/ Egg Proteins - metabolism
/ Fundamental and applied biological sciences. Psychology
/ Generally accepted auditing standards
/ Hydroxyapatites - metabolism
/ Miscellaneous
/ Molecular Sequence Data
/ Osteonectin
/ Ovomucin - metabolism
/ Proteins
/ Sequencing
/ Serine Proteinase Inhibitors
/ Ungulates
1988
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Osteonectin cDNA Sequence Reveals Potential Binding Regions for Calcium and Hydroxyapatite and Shows Homologies with Both a Basement Membrane Protein (SPARC) and a Serine Proteinase Inhibitor (Ovomucoid)
Journal Article
Osteonectin cDNA Sequence Reveals Potential Binding Regions for Calcium and Hydroxyapatite and Shows Homologies with Both a Basement Membrane Protein (SPARC) and a Serine Proteinase Inhibitor (Ovomucoid)
1988
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Overview
Osteonectin is a prominent noncollagenous protein of developing bone. A 2150-base-pair cDNA coding for osteonectin, isolated from a bovine bone cell λ gt11 expression library, was sequenced and identified by comparison with protein sequence data. The nucleotide sequence predicts that osteonectin contains 304 amino acids, including a 17-residue signal peptide. Analysis of the deduced protein sequence suggests that the secreted protein contains at least four distinct structural domains. An acidic region at the amino terminus of the protein appears to be a potential hydroxyapatite-binding site. This is followed by a second domain, rich in cysteine, that shows sequence homology with cysteine-rich domains in turkey ovomucoid and other serine proteinase inhibitors. Two sequences homologous with central calcium-binding loops of ``EF hands'' and thus having potential to be high-affinity calcium-binding sites are located in two other domains within the carboxyl-terminal half of the protein. Finally, the osteonectin sequence shows near identity (>90%) with another protein, SPARC (secreted protein, acidic and rich in cysteine), secreted by mouse parietal endoderm. These data suggest that osteonectin, a protein present in bone and other selected tissues, is a multifunctional protein.
Publisher
National Academy of Sciences of the United States of America,National Acad Sciences
Subject
/ Analytical, structural and metabolic biochemistry
/ Animals
/ Biological and medical sciences
/ Bones
/ Calcium
/ Carrier Proteins - metabolism
/ Cattle
/ Fundamental and applied biological sciences. Psychology
/ Generally accepted auditing standards
/ Hydroxyapatites - metabolism
/ Proteins
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