Biochemical and Biophysical Research Communications
Regular ArticleProduction of Human PTH(1-34) via a Recombinant DNA Technique
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Pharmacological effects of a recombinant hPTH(1−34) derived peptide on ovariectomized rats
2017, European Journal of PharmacologyCitation Excerpt :Intermittent administration of hPTH has been shown to be able to enhance bone formation (Nakagawa et al., 1994; Whitfield et al., 1995), restore weakened bone affected with osteoporosis to its normal strength and density in small animals (Fox et al., 2006). In addition, some of its shorter degradation products also possess this activity, such as hPTH(1−34), the N-terminal 1–34 amino acid fragment of human parathyroid hormone, which has full biological activity of the holohormone hPTH(1−84) for postmenopausal women with osteoporosis (Nakagawa et al., 1994). It has been approved that by protein engineering, local modification can be carried out on natural protein or peptide, and some of the modified protein/peptide may obtain enhanced potency to improve the human health.
Expression, purification, and PC1-mediated processing of human proglucagon, glicentin, and major proglucagon fragment
2003, Protein Expression and PurificationPrevention of bone loss in ovariectomized rats by pulsatile transdermal iontophoretic administration of human PTH(1-34)
2002, Journal of Pharmaceutical SciencesCitation Excerpt :Powders of hPTH(1–34) hydrochloride (relative purity as analyzed by HPLC, > 99%) were obtained from Discovery Research Laboratories, Takeda Chemical Ind. Ltd., and were produced by fragmenting the recombinant hPTH(1–84).15 A user‐activated iontophoretic administration device (Figure 1) was used for the iontophoretic administration of hPTH(1–34) to the rats.
Optimization of the cleavage reaction for cyanylated cysteinyl proteins for efficient and simplified mass mapping
1998, Analytical Biochemistry