Synthesis of fully active biotinylated analogs of parathyroid hormone and parathyroid hormone-related protein as tools for the characterization of parathyroid hormone receptors

Biochemistry ◽  
1992 ◽  
Vol 31 (16) ◽  
pp. 4026-4033 ◽  
Author(s):  
Eliahu Roubini ◽  
Le T. Duong ◽  
Susan W. Gibbons ◽  
Chih T. Leu ◽  
Michael P. Caulfield ◽  
...  
1989 ◽  
Vol 264 (25) ◽  
pp. 14806-14811
Author(s):  
R G Hammonds ◽  
P McKay ◽  
G A Winslow ◽  
H Diefenbach-Jagger ◽  
V Grill ◽  
...  

1996 ◽  
Vol 271 (40) ◽  
pp. 24371-24381 ◽  
Author(s):  
Terence L. Wu ◽  
Rupangi C. Vasavada ◽  
Kai Yang ◽  
Thierry Massfelder ◽  
Michael Ganz ◽  
...  

1990 ◽  
Vol 322 (16) ◽  
pp. 1106-1112 ◽  
Author(s):  
William J. Burtis ◽  
Thomas G. Brady ◽  
John J. Orloff ◽  
Julie B. Ersbak ◽  
Raymond P. Warrell ◽  
...  

1990 ◽  
Vol 127 (1) ◽  
pp. 167-176 ◽  
Author(s):  
W. A. Ratcliffe ◽  
E. Green ◽  
J. Emly ◽  
S. Norbury ◽  
M. Lindsay ◽  
...  

ABSTRACT Parathyroid hormone-related protein (PTHrP) was measured in human and bovine milk by radioimmunoassay (RIA) and bioassay, and the molecular forms characterized by gel chromatography and immunoblotting of affinity-purified PTHrP. Mean immunoreactive PTHrP(1–34) concentrations were 23 and 87 μg/l in human and bovine milk respectively. Bioactive (BIO) PTHrP concentrations determined by cyclic AMP production by ROS 17/2·8 cells correlated significantly (P< 0·001) with those obtained by RIA (BIO = 1·04RIA−3·4, r = 0·939). Gel filtration of human and bovine milk identified several peaks with immunoactivity and bioactivity. Immunoblotting of affinity-purified PTHrP revealed multiple molecular species including components with mobilities similar to those of PTHrP and its subfragments. These studies confirm the presence of immuno- and bioactive PTHrP in milk and suggest that post-translational processing is complex and variable. Journal of Endocrinology (1990) 127, 167–176


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