Title : Full mass spectrometric characterization of human monoacylglycerol lipase generated by large-scale expression and single-step purification.

Pub. Date : 2008 May

PMID : 18452279






5 Functional Relationships(s)
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Protein Name
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1 With 2-AG as substrate, hMGL displayed an apparent V max of 25 micromol/(microg min) and K m of 19.7 microM, an affinity for 2-AG similar to that of native rat-brain MGL (rMGL) (Km=33.6 microM). glyceryl 2-arachidonate monoglyceride lipase Rattus norvegicus
2 With 2-AG as substrate, hMGL displayed an apparent V max of 25 micromol/(microg min) and K m of 19.7 microM, an affinity for 2-AG similar to that of native rat-brain MGL (rMGL) (Km=33.6 microM). glyceryl 2-arachidonate monoglyceride lipase Rattus norvegicus
3 hMGL also demonstrated a comparable affinity (Km approximately 8-9 microM) for the novel fluorogenic substrate, arachidonoyl, 7-hydroxy-6-methoxy-4-methylcoumarin ester (AHMMCE), in a sensitive, high-throughput fluorometric MGL assay. arachidonoyl monoglyceride lipase Rattus norvegicus
4 hMGL also demonstrated a comparable affinity (Km approximately 8-9 microM) for the novel fluorogenic substrate, arachidonoyl, 7-hydroxy-6-methoxy-4-methylcoumarin ester (AHMMCE), in a sensitive, high-throughput fluorometric MGL assay. 7-hydroxy-6-methoxy-4-methylcoumarin ester monoglyceride lipase Rattus norvegicus
5 hMGL also demonstrated a comparable affinity (Km approximately 8-9 microM) for the novel fluorogenic substrate, arachidonoyl, 7-hydroxy-6-methoxy-4-methylcoumarin ester (AHMMCE), in a sensitive, high-throughput fluorometric MGL assay. ahmmce monoglyceride lipase Rattus norvegicus