Zobrazeno 1 - 10
of 11
pro vyhledávání: '"S K, Nishimoto"'
Publikováno v:
Journal of materials science. Materials in medicine. 12(8)
This study examined the spatial distribution of selected biochemical and mechanical properties along the length of carp rib bone. Carp rib bone was chosen because of its unusually high osteocalcin content relative to other extractable proteins. The a
Publikováno v:
Journal of biomedical materials research. 54(4)
Osteocalcin is one of the most abundant noncollagenous proteins in bone. It is strongly associated with the mineral phase of bone, and has long been associated as a marker of bone turnover. However, its relationship to bone composition, strength, and
Autor:
C. A. Titchenal, S K. Nishimoto
Publikováno v:
Medicine & Science in Sports & Exercise. 33:S339
Autor:
S K Nishimoto, P A Price
Publikováno v:
Journal of Biological Chemistry. 254:437-441
Publikováno v:
The Journal of biological chemistry. 255(7)
Publikováno v:
Clinical orthopaedics and related research. (234)
Ectopic bone formation induced by the subcutaneous implantation of demineralized bone matrix (DBM) is very significantly reduced in older Fischer 344 rats. Cells originating from calvaria of 20-day-old embryo donors were introduced into cylinders of
Autor:
S K, Nishimoto, S M, Padilla
Publikováno v:
Progress in clinical and biological research. 287
Publikováno v:
The Journal of biological chemistry. 257(18)
The nature of the proteoglycan antigen which accumulates in chick embryo chondrocytes that had been incubated in monensin was examined. Both the culture media and cell lysates were immunoprecipitated using antibody which primarily is directed against
Publikováno v:
The Journal of biological chemistry. 257(19)
Detailed studies of the effects of the ionophore monensin upon avian chondrocyte ultrastructure, macromolecular synthesis, and macromolecular secretion have been carried out. Embryonic avian chondrocytes in suspension culture were incubated in concen
Publikováno v:
The Journal of biological chemistry. 258(1)
Detailed studies of the effects of the ionophore monensin upon the glycosylation of secreted fibronectin have been carried out. Human fibroblasts in culture were incubated in 1 microM monensin for several hours, following which radiolabeled glucosami