Immunohistochemical localization of a ∼66 kD glycosylated phosphoprotein during development of the embryonic chick tibia

1991 ◽  
Vol 48 (6) ◽  
pp. 429-437 ◽  
Author(s):  
Scott P. Bruder ◽  
Arnold I. Caplan ◽  
Yozoh Gotoh ◽  
Louis C. Gerstenfeld ◽  
Melvin J. Glimcher
Keyword(s):  
Immunohistochemical Localization ◽  
Embryonic Chick ◽  
Chick Tibia

The in Vitro Effect of Insulin on Collagen Synthesis in Embryonic Chick Tibia

1973 ◽  
Vol 142 (4) ◽  
pp. 1152-1154 ◽  
Author(s):  
J. S. Perlish ◽  
R. I. Bashey ◽  
R. Fleischmajer
Keyword(s):  
Collagen Synthesis ◽  
Embryonic Chick ◽  
Chick Tibia ◽  
Vitro Effect

scholarly journals Immunohistochemical localization of AMPA-type glutamate receptor subunits in the nucleus of the Edinger-Westphal in embryonic chick

2011 ◽  
Vol 498 (3) ◽  
pp. 199-203
Author(s):  
Claudio A.B. Toledo ◽  
Anton Reiner ◽  
Reena S. Patel ◽  
Adriane W. Vitale ◽  
Jordan M. Klein ◽  
...  
Keyword(s):  
Glutamate Receptor ◽  
Immunohistochemical Localization ◽  
Embryonic Chick

scholarly journals Immunohistochemical Localization of Netrin-1 in the Embryonic Chick Nervous System

1997 ◽  
Vol 17 (14) ◽  
pp. 5466-5479 ◽  
Author(s):  
A. John MacLennan ◽  
Diana L. McLaurin ◽  
Lianne Marks ◽  
Emily N. Vinson ◽  
Marylynn Pfeifer ◽  
...  
Keyword(s):  
Nervous System ◽  
Immunohistochemical Localization ◽  
Embryonic Chick

scholarly journals Post-translational processing of chicken bone phosphoproteins. Identification of bone (phospho)protein kinase

1990 ◽  
Vol 268 (3) ◽  
pp. 593-597 ◽  
Author(s):  
Y Mikuni-Takagaki ◽  
M J Glimcher
Keyword(s):  
Protein Kinase ◽  
Bone Tissue ◽  
Potential Role ◽  
Polyacrylamide Gel ◽  
Catalytic Subunit ◽  
Regulatory Mechanisms ◽  
Embryonic Chick ◽  
Chick Tibia

We have detected a protein kinase which phosphorylates bone phosphoproteins (BPPs) in the detergent extract of the membranous fractions in the periosteal bone strips of 12-day-embryonic-chick tibia. This enzyme, tentatively named BPP kinase, has a catalytic subunit of Mr approximately 39,000, utilizes GTP as well as ATP as a phospho-group donor, is inhibited by 2,3-bisphosphoglycerate and heparin, and is therefore similar to casein kinase II. The enzyme can phosphorylate dephosphorylated proteins such as casein, phosvitin and chicken BPPs, but the last-named are preferred substrates. The in vitro-phosphorylation-assay products of this enzyme in the extract were indistinguishable on an SDS/polyacrylamide gel from the major [32P]phosphoproteins metabolically labelled in the embryonic-chick bone tissue. The regulatory mechanisms of the phosphorylation process of BPPs by BPP kinase as well as the potential role of this enzyme in mineralization are discussed.

Effect of weak inductively coupled pulsating currents on calcium uptake in embryonic chick tibia explants

1981 ◽  
Vol 128 ◽  
pp. 515-521
Author(s):  
J. Assailly ◽  
J.-D. Monet ◽  
Y. Goureau ◽  
P. Christel ◽  
A.A. Pilla
Keyword(s):  
Calcium Uptake ◽  
Embryonic Chick ◽  
Inductively Coupled ◽  
Chick Tibia

The influence of bone and marrow on cartilage hypertrophy and degradation during 30-day serum-free culture of the embryonic chick tibia

1992 ◽  
Vol 193 (3) ◽  
pp. 277-285 ◽  
Author(s):  
Ada A. Cole ◽  
Lawrence J. Luchene ◽  
Thomas F. Linsenmayer ◽  
Thomas M. Schmid
Keyword(s):  
Embryonic Chick ◽  
Serum Free ◽  
Chick Tibia

scholarly journals Hydroxylysine in the N-terminal regions of the α1- and α2-chains of various collagens

1971 ◽  
Vol 125 (2) ◽  
pp. 433-437 ◽  
Author(s):  
M. J. Barnes ◽  
B. J. Constable ◽  
L. F. Morton ◽  
E. Kodicek
Keyword(s):  
Frontal Bone ◽  
Lysine Residue ◽  
Embryonic Chick ◽  
Tibia Bone ◽  
Rat Tibia ◽  
Chick Tibia ◽  
Tail Tendon ◽  
High Degree ◽  
Rat Tail ◽  
Tendon Collagen

The degree of hydroxylation of the lysine residue located in both α1- and α2-chains of collagen in the N-terminal, non-helical telopeptide region of the molecule has been determined in collagen from various sources after isolation of the peptides (α1- and α2-CB1) that contain the lysine residue in question and are obtained by cyanogen bromide cleavage of collagen α1- and α2-chains respectively. As with collagen from chick tibia, bone collagens from rat tibia and femur and embryonic chick frontal bone, have a high degree of hydroxylation (approx. 50% or more) of the lysine residue in both α1- and α2-CB1 peptides. This is in contrast with the lack of hydroxylation of this residue in both α1- and α2-chains of all skin collagens so far examined. The presence of hydroxylysine in α1- and α2-CB1 peptides from tendon collagen is also indicated. In rat tail tendon collagen the amount of hydroxylation is only slight but in the much less soluble tendon collagen from embryonic chick leg tendons, approximately one-third of the lysine is hydroxylated.

Type X Collagen Degradation in Long-Term Serum-Free Culture of the Embryonic Chick Tibia Following Production of Active Collagenase and Gelatinase

1993 ◽  
Vol 159 (2) ◽  
pp. 528-534 ◽  
Author(s):  
Ada A. Cole ◽  
Tahira Boyd ◽  
Lawrence Luchene ◽  
Klaus E. Kuettner ◽  
Thomas M. Schmid
Keyword(s):  
Collagen Degradation ◽  
Embryonic Chick ◽  
Type X Collagen ◽  
Serum Free ◽  
Active Collagenase ◽  
Chick Tibia
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