{'fraction_non_alphanumeric': 0.024810475534114404, 'fraction_numerical': 0.007580978635423846, 'mean_word_length': 5.23175965665236, '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}}
Application of anaerobic ion-exchange chromatography to the separation of hemoglobins in R from T conformational states.

As an allosteric protein, hemoglobin can assume at least two different quatenary structures, a deoxy or T for tense conformation and an oxy or R for relaxed conformation (2,3) depending upon its state of ligation. Because the pK values of oxy and deoxy- hemoglobins are different, molecules in the R conformation should behave differently than molecules in the T conformation on ion exchange chromatography. Kilmartin et al. (4) designed an anaerobic cation exchange chromatographic procedure with which they separated the deoxy hemoglobin from oxy hemoglobin and other R conformation hemoglobin components like CO-hemoglobin and sulfohemoglobin. In this report we describe the further development of Kilmartin's procedure to separate two electrophoretically silent hemoglobin mutants, Hb Potomac [beta 101 Glu leads to Asp] (5) a high oxygen affinity variant, and Hb M-Milwaukee [beta 67 Val leads to Glu] (6,8) a low oxygen affinity mutant from Hb A. The modifications we have made include (a) applying the hemolysate at a partial pressure of oxygen determined from an examination of the oxygen equilibrium curve to produce a favorable ratio of T to R conformations of the two hemoglobins to be separated, (b) controlling the partial pressure of oxygen tension of the column effluent during the development of the chromatogram.