Differences in the glycosylation of recombinant and native human milk bile salt-stimulated lipase revealed by peptide mapping.
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[1] O. Hernell,et al. Recombinant human milk bile salt-stimulated lipase. Catalytic activity is retained in the absence of glycosylation and the unique proline-rich repeats. , 1993, The Journal of biological chemistry.
[2] J. Holgersson,et al. Glycosylation of extracellular superoxide dismutase studied by high-performance liquid chromatography and mass spectrometry. , 1991, Journal of chromatography.
[3] C. S. Wang,et al. Structure of human milk bile salt activated lipase. , 1991, Biochemistry.
[4] P. Carlsson,et al. cDNA cloning of human-milk bile-salt-stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase. , 1990, European journal of biochemistry.
[5] O. Hernell,et al. The bile-salt-stimulated lipase in human milk. Purification and characterization. , 1981, European journal of biochemistry.
[6] O. Hernell. III. Physiological Implications of the Bile Salt‐Stimulated Lipase , 1975, European journal of clinical investigation.
[7] T. Olivecrona,et al. Human milk lipases. II. Bile salt-stimulated lipase. , 1974, Biochimica et biophysica acta.
[8] S. Carr,et al. Structural classification of carbohydrates in glycoproteins by mass spectrometry and high-performance anion-exchange chromatography. , 1991, Analytical biochemistry.