Abstract
An acid phosphatase with optimum pH at 6 was found in the total albumin extract of mature dry Lupinus albus seeds. Three groups of phosphatase isoenzymes were identified by IEF. The active bands in the IEF gel were run in 2D-SDS-PAGE under reducing conditions and found to contain one major ( ca 70%) polypeptide chain of M r 68 000 and one minor ( ca 30%) of 61 000. When lupin seeds were incubated in water for 3 hr at 60°, residual phosphatase activity was detectable in the medium suggesting that the enzyme was secreted together with other already identified polypeptides. The IEF and 2D-SDS-PAGE patterns of the constitutive and heat-secreted phosphatase(s) coincided.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
