Comparison of the properties of phosphoglucomutase from muscle of turbot (Reinhardtius hippoglossoides, Greenland Halibut) and witch flounder (Glyptocephalus cynoglossus) from the Northwest Atlantic and the Gulf of St. Lawrence.
1. Phosphoglucomutase from muscle of turbot and witch has been purified and the properties studied from two regions of the Northwest Atlantic and the Gulf of St. Lawrence. 2. The enzyme, purified 157 fold from turbot and 164 fold from witch had specific activities of 596 and 475 U/mg/min respectively. 3. The M.W. and pH optimum of the enzyme from both species were 63,500 and 7500; and 63,000 and 7800 for the Northwest Atlantic and the Gulf samples respectively. 4. The amino acid contents and responses towards different inhibitory agents were different for the enzyme from the Gulf than the Northwest Atlantic samples. 5. The findings compares well with the genetic analysis of the electrophoretic properties of the enzyme in relation to stock discrimination of the two species.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002170:Canada; D005399:Fishes / Q000378:metabolism*; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D010733:Phosphoglucomutase / Q000302:isolation & purification / Q000378:metabolism*; D012623:Seawater; D013045:Species Specificity
D000596:Amino Acids; D010733:Phosphoglucomutase