Proceedings of the National Academy of Sciences · 1987 · 739 citations · 26 references
Life SciencesBiochemistryMolecular BiologyHormone BiochemistryProtein BiochemistryProteomicsParathyroid Gland PhysiologyParathyroid Hormone PhysiologyAmino Acid AnalysisCancer Cell Line ModelsParathyroid Hormone BiologySerum-free Cell CultureSerum-free CultureSerum-free Culture MediaSynthetic Peptide Characterization
A protein with biological activities similar to parathyroid hormone (PTH) has been purified from serum-free culture medium obtained from a human lung cancer cell line (BEN). A major protein band of 18 kDa was obtained on NaDodSO4/polyacrylamide gels, with faint bands at 35 kDa and 67 kDa. Biological activity was associated only with the 18-kDa band. Amino acid sequence analysis of the material purified by HPLC revealed that 8 of the 16 residues were identical with those of human PTH. Antibody raised to a corresponding synthetic peptide recognized the PTH-related material but showed less than 1% cross-reactivity with human PTH amino-terminal peptides. BEN cells contained PTH DNA, but not PTH messenger RNA, indicating involvement of another gene. The purified PTH-related protein had a specific biological activity approximately equal to 6 times greater than that of bovine PTH(1-34). The PTH-related protein may have a role in the syndrome of humoral hypercalcemia of malignancy.
26
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations
Haider Raza, Annie John, Abderrahim Nemmar · Cellular Physiology and Biochemistry · 2013 · 47.3K citations · Full text
Rapid transfer of DNA from agarose gels to nylon membranes
Ken C. Reed, David A. Mann · Nucleic Acids Research · 1985 · 1.8K citations · Full text