Summary Ion‐exchange chromatography on DEAE‐Sephacel revealed the presence of two forms of glutamine synthestase (GSI and GSII) in leaf tissue and one form in root tissue of the angiosperm halophyte, Triglochin maritima. The chromatographic characteristics of GSI and the root enzyme were similar but there were differences in their stability, GSI being considerably more stable than the root enzyme. The characteristics of GSI and GSII exhibited some differences, GSII showed negative cooperativity with respect to glutamate and had a pH optimum of 8−0 compared with 7.2 for GSI. GSI was found to be unstable, particularly in the presence of inorganic salts. Compounds such as glycine betaine, proline and sorbitol, which are thought to function as compatible osmotic solutes in halophytes, were found to stabilize GSII.
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Ahmad et al. (1982) studied this question.
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