Chromatofocusing of N-terminally processed forms of proteins. Isolation and characterization of two forms of interleukin-1 beta and of bovine growth hormone.
Using chromatofocusing, two fractions have been obtained from recombinant-derived interleukin-1 beta (IL-1 beta) and from pituitary-derived bovine growth hormone (BGH). The forms of both proteins responsible for these fractions have been characterized by N-terminal and C-terminal amino acid sequence determination. Recombinant IL-1 beta, as a mixture of correctly processed polypeptide and an N-terminally methionylated form, was resolved rapidly by chromatofocusing. BGH was resolved into the full-length polypeptide commencing Ala-Phe-Pro-Ala-Met-Ser-Leu- and a form truncated at the N-terminus by four amino acid residues, which thus commences Met-Ser-Leu-; the fraction containing the truncated form also contains a species having N-terminal Phe-Pro-Ala-. These results, and the possible generality of the separation, are discussed.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D008401:Gas Chromatography-Mass Spectrometry; D013006:Growth Hormone / Q000302:isolation & purification*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007375:Interleukin-1 / Q000302:isolation & purification*; D007525:Isoelectric Focusing; D011506:Proteins / Q000302:isolation & purification*
D007375:Interleukin-1; D011506:Proteins; D013006:Growth Hormone