{'fraction_non_alphanumeric': 0.01911220715166461, 'fraction_numerical': 0.004315659679408138, 'mean_word_length': 5.995689655172414, '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}}
Leucocyte Glycogen Response in Inflammatory Exudates

Summary. Leucocyte glycogen responses in inflammatory exudates were studied in guinea‐pigs. Inflammatory exudates were produced by sterile casein injection intraperitoneally. Glycogen content, incorporation of [14C]glucose into glycogen, and activity of glycogen synthetase and glycogen phosphorylase were studied in both exudate leucocytes and blood leucocytes of the same animals. Glycogen content rises dramatically in exudate leucocytes and remains above control blood values for at least 5 days. Glycogen content of circulating blood leucocytes also rises to less extreme but significant levels during inflammation. Fasting had no effect on the ability of the animals to sustain the glycogen‐loading response in the leucocytes over a 3‐day period. Incorporation of [14C]glucose into glycogen was low in exudate leucocytes and high in blood leucocytes. An inverse correlation between glycogen content and glucose incorporation into leucocyte glycogen was demonstrated for exudate leucocytes. Glycogen synthetase activity was found significantly higher in exudate leucocytes than blood leucocytes, the increase being primarily in the glucose‐6‐phosphate‐dependent (D) form of the enzyme. Glycogen phosphorylase activity was no different in blood and exudate leucocytes. The striking rise in glycogen content of inflammatory leucocytes is probably part of a normal physiologic response, and can be accounted for by a relative increase in glycogen synthesis (synthetase activity) while glycogen degradation in these constantly turning‐over molecules remains constant.