{'fraction_non_alphanumeric': 0.024324324324324326, 'fraction_numerical': 0.014864864864864866, 'mean_word_length': 5.170833333333333, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Acyl carrier protein. 28. Chemical synthesis and characterization of a protein with acyl carrier protein activity.

Abstract A protected linear polypeptide of 74 amino acids with the sequence of Escherichia coli 1 to 74 apo-acyl carrier protein (ACP) was synthesized by the automated solid phase method. The polypeptide was removed from the solid support and partially deprotected by treatment of the peptide-resin with hydrogen bromide and trifluoroacetic acid, and the product was purified by gel filtration. The removal of protecting groups was completed by hydrogenation, and the prosthetic group, 4'-phosphopantetheine, was introduced enzymatically with holo-ACP synthetase. Ion exchange chromatography of the product yielded a preparation in which 55% of the protein in the purified fraction contained the prosthetic group. This synthetic 1 to 74 holo-ACP was as active as native holo-ACP in the malonyl pantetheine-CO2 exchange reaction which is dependent upon malonyl-coenzyme A-ACP transacylase and β-ketoacyl-ACP synthetase. The purified synthetic 1 to 74 holo-ACP preparation was found to be homogeneous and similar to native 1 to 74 holo-ACP as judged by co-chromatography on DEAE-cellulose and Sephadex G-50 and by sodium dodecyl sulfate disc gel electrophoresis. In addition the synthetic and native proteins were similar with respect to their ultraviolet spectra, amino acid compositions, and their immunological activity with antiserum prepared against native ACP.