Structural Studies of Parathyroid Hormone Analogue with C-Terminal Aldehyde Function

2009 ◽  
pp. 61-62
Author(s):  
Zhanna Potetinova ◽  
Feng Ni ◽  
Ping Xu ◽  
Gordon E. Willick
Keyword(s):  
Parathyroid Hormone ◽  
Structural Studies ◽  
Hormone Analogue

scholarly journals In Vitro & In Vivo Effect of Parathyroid Hormone Analogue (1-14) Containing α-amino-iso-butyric Acid Residue (Aib)1,3

2006 ◽  
Vol 47 (2) ◽  
pp. 214 ◽  
Author(s):  
Yumie Rhee ◽  
Weontae Lee ◽  
Eun Jin Lee ◽  
Suhyun Ma ◽  
So Young Park ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Butyric Acid ◽  
Hormone Analogue

Evaluation of a parathyroid hormone antagonist in an in vivo multiparameter bioassay

1987 ◽  
Vol 253 (2) ◽  
pp. E187-E192
Author(s):  
N. Horiuchi ◽  
M. Rosenblatt
Keyword(s):  
Parathyroid Hormone ◽  
Dependent Manner ◽  
Hydroxylase Activity ◽  
Dose Ratio ◽  
Hormone Analogue ◽  
Potent Antagonist ◽  
Dose Dependent ◽  
Bovine Parathyroid Hormone ◽  
Stimulation Of

The antagonist properties of a bovine parathyroid hormone analogue ([Tyr34]bPTH-(7-34] amide were quantitatively assessed in vivo in a multiparameter assay to estimate the potency of the antagonist against the major actions of PTH. The analogue inhibited PTH-stimulated urinary excretion of phosphate and adenosine 3',5'-cyclic monophosphate in vitamin D-deficient thyroparathyroidectomized rats in a dose-dependent manner. At a molar dose ratio as low as 5:1 of antagonist to PTH, partial inhibition occurred. PTH stimulates the activity of 25-hydroxyvitamin D3-1 alpha-hydroxylase in renal proximal tubules. When coinfused with PTH, this analogue completely inhibited PTH-stimulated 1 alpha-hydroxylase activity at a molar dose ratio of 25:1 of antagonist to PTH and partially inhibited the activity at a molar dose ratio of 10:1. The analogue revealed no PTH-like agonist activity for stimulation of the 1 alpha-hydroxylase. Taken together, these studies indicate that [Tyr34]bPTH-(7-34) amide is a potent antagonist of several of the parameters of PTH action in vivo and demonstrate the feasibility of designing a PTH antagonist that can interact simultaneously with all the PTH receptors responsible for the hormone's major actions in vivo.

scholarly journals Repurposing a novel parathyroid hormone analogue to treat hypoparathyroidism

2017 ◽  
Vol 175 (2) ◽  
pp. 262-271 ◽  
Author(s):  
Venkatesh Krishnan ◽  
Yanfei L Ma ◽  
Catherine Z Chen ◽  
Natasha Thorne ◽  
Heather Bullock ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Hormone Analogue

Internal ribosome-binding site directs expression of parathyroid hormone analogue (8–84) in Escherichia coli

1991 ◽  
Vol 181 (1) ◽  
pp. 481-485 ◽  
Author(s):  
Wing L. Sung ◽  
Cathy K. Luk ◽  
Diana M. Zahab ◽  
Jean R. Barbier ◽  
Marc Lafontaine ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Parathyroid Hormone ◽  
Binding Site ◽  
Ribosome Binding Site ◽  
Hormone Analogue ◽  
Ribosome Binding

Ribosome Structural Organization

1974 ◽  
Vol 32 ◽  
pp. 332-333
Author(s):  
James A. Lake
Keyword(s):  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Small Subunit ◽  
Structural Studies ◽  
X Ray Diffraction ◽  
Specific Antibodies ◽  
X Ray ◽  
E Coli ◽  
Complete Sequences

The understanding of ribosome structure has advanced considerably in the last several years. Biochemists have characterized the constituent proteins and rRNA's of ribosomes. Complete sequences have been determined for some ribosomal proteins and specific antibodies have been prepared against all E. coli small subunit proteins. In addition, a number of naturally occuring systems of three dimensional ribosome crystals which are suitable for structural studies have been observed in eukaryotes. Although the crystals are, in general, too small for X-ray diffraction, their size is ideal for electron microscopy.

Structural Studies on Mitotic Spindle Fibres

1978 ◽  
Vol 36 (3) ◽  
pp. 615-626
Author(s):  
J.R. Mcintosh
Keyword(s):  
Chemical Composition ◽  
Mitotic Spindle ◽  
Structural Studies ◽  
Mitotic Apparatus ◽  
Chemical Studies ◽  
Medical Interest ◽  
Spindle Fibres

The mitotic apparatus is a structure of obvious biological and medical interest, but it has proved to be a difficult cellular machine to understand. The chemical composition of the spindle is only slightly elucidated, largely because of the difficulties in preparing useful isolates of the structure. Chemical studies of the mitotic spindle have been reviewed elsewhere (Mcintosh, 1977), and will not be discussed further here. One would think that structural studies on the mitotic apparatus (MA) in situ would be straightforward, but even with this approach there is some disagreement in the results obtained with various methods and by different investigators. In this paper I will review briefly the approaches which have been used in structural studies of the MA, pointing out the strengths and problems of each approach. I will summarize the principal findings of the different methods, and identify what seem to be fruitful avenues for further work.

Image registration with a computer driven S.T.E.M.

1978 ◽  
Vol 36 (1) ◽  
pp. 98-99
Author(s):  
A.M.H. Schepman ◽  
J.A.P. van der Voort ◽  
J.E. Mellema
Keyword(s):  
Spot Size ◽  
Scanning Transmission Electron Microscope ◽  
Small Computer ◽  
Structural Studies ◽  
Area Of Interest ◽  
Transmission Electron ◽  
Scanning Transmission ◽  
Specimen Area ◽  
On Line ◽  
Minimum Distances

A Scanning Transmission Electron Microscope (STEM) was coupled to a small computer. The system (see Fig. 1) has been built using a Philips EM400, equipped with a scanning attachment and a DEC PDP11/34 computer with 34K memory. The gun (Fig. 2) consists of a continuously renewed tip of radius 0.2 to 0.4 μm of a tungsten wire heated just below its melting point by a focussed laser beam (1). On-line operation procedures were developped aiming at the reduction of the amount of radiation of the specimen area of interest, while selecting the various imaging parameters and upon registration of the information content. Whereas the theoretical limiting spot size is 0.75 nm (2), routine resolution checks showed minimum distances in the order 1.2 to 1.5 nm between corresponding intensity maxima in successive scans. This value is sufficient for structural studies of regular biological material to test the performance of STEM over high resolution CTEM.

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