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A human prostatic growth factor (hPGF): Partial purification and characterization

✍ Scribed by Nozomu Nishi; Yuhsi Matuo; Yasuyoshi Muguruma; Yoshino Yoshitake; Katsuzo Nishikawa; Fumio Wada


Book ID
115759196
Publisher
Elsevier Science
Year
1985
Tongue
English
Weight
373 KB
Volume
132
Category
Article
ISSN
0006-291X

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Partial purification and characterizatio
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A growth factor capable of stimulating DNA synthesis of Balb/c 3T3 cells was purified by heparin-Sepharose column chromatography about 1900-fold from the cytosol of human prostatic tissues obtained at autopsy or open prostatectomy. This growth factor bound to heparin-Sepharose in the presence of 0.5

Characterization and partial purificatio
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A polypeptide growth factor has been partially purified from medium conditioned by the human adrenocortical carcinoma cell line SW13. This factor, designated h-TGFe, stimulates anchorage-independent growth of the SW13 cells. Similar activity was observed in human milk, and in conditioned media from

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## Abstract A purification procedure and partial characterization of bovine pituitary fibroblast growth factor (FGF) are described. The steps of the published methods [3,4] which yield inhomogeneous material, were retained, with modifications. The final isolation, with an additional purification of

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Human recombinant EGF, secreted into the extracellular medium by E. c&i cells, was purified by a combination of solid phase extraction and HPLC. Using these techniques, the peptide was purified 122-fold, with a recovery of greater than 75%. The purified hEGF manifested no contaminating protein bands