These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Purification of human milk bile salt-activated lipase.
    Author: Wang CS, Johnson K.
    Journal: Anal Biochem; 1983 Sep; 133(2):457-61. PubMed ID: 6638506.
    Abstract:
    A modified procedure for a large-scale purification of human milk bile salt-activated lipase (BAL) has been devised. An initial step used cholate-Sepharose affinity chromatography for the partial purification of the enzyme followed by the removal of cholate with a Bio-Rex 5 anion-exchange resin. The final step of purification used heparin-Sepharose affinity chromatography. This procedure of purification resulted in a 50-fold purification of BAL from human skim milk and a specific activity of 50-60 mumol/min/mg with p-nitrophenyl acetate as substrate. From 450 ml of human skim milk, approximately 30 mg of purified enzyme could be obtained. The N-terminal-region amino acid sequence of the purified BAL was determined as follows: Ala-Lys-Leu-Gly-Ala-Val-Tyr-Thr-Glu-Gly-Lys-Phe-Val-Glu-Gly-Val-Asn-Lys-Lys-Leu-Gly-Leu-. Despite the finding that BAL interacts with heparin-Sepharose, soluble heparin had no effect on BAL activity. The possible physiological role of BAL-heparin interaction has also been discussed.
    [Abstract] [Full Text] [Related] [New Search]