93 research outputs found
Isolation of a somatomedin binding protein from human preterm amniotic fluid : development of a radioimmunoassay
This thesis study was undertaken in order to investigate
the nature and biological behavior of a somatornedin
binding protein, identified in preterrn amniotic fluid (AF).
Somatomedin (SM) is the generic designation applied to
a family of serum peptide growth factors which are growth
hormone dependent, stimulate incorporation of sulphate
into cartilage, have insulin-like actions on nonskeletal
tissues and increase mitosis in a wide variety of cultured
cells. Thusfar two peptides have been fully characterized:
insulin-like growth factor I (IGF-I), shown to be identical
to sornatomedin-C, and insulin-like growth factor II
(IGF-II). IGF-I and IGF-II have a 62% aminoacid sequence
identity and are 38-48% homologous with the A and B domains
of human pro-insulin
Site-directed mutagenesis of the N-terminal region of IGF binding protein 1; analysis of IGF binding capability
AbstractTo define domains involved in IGF binding 60 N-terminal amino acid residues of IGFBP-1 were deleted. This deletion resulted in loss of IGF binding suggesting that the N-terminus may enclose an IGF binding domain. However, most point mutations introduced in this region did not affect IGF binding. In contrast to Cys-34, only substitution of Cys-38 for a tyrosine residue abolished IGF binding. With the determination that all 18 cysteine residues are involved in disulphide bond formation our data suggest that, although not all cysteines contribute to the same extent, the ligand binding site may be spatially organized
Effects of Alternate-day or Daily Prednisone Treatment on GH and Cortisol Levels in Growth-Retarded Children after Renal Transplantation
A Scoping Review of the use of E-Learning and E-Consultation for Healthcare Workers in Low-and-Middle-Income Countries and their potential Complementarity
Prevention, Population and Disease management (PrePoD)Public Health and primary car
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