A comparative study of enzymatic digestion profiles of apolipoprotein B from four human subjects.
A methodological approach for comparative structural study of apolipoprotein B has been developed. Low-density lipoproteins from four human subjects were digested in three separate enzyme systems, utilizing trypsin, chymotrypsin and Staphylococcus aureus protease V8, each in the presence of 1% sodium dodecyl sulfate. The peptides were separated by electrophoresis on polyacrylamide gels in SDS; the stained gels were scanned spectrophotometrically to produce characteristic profiles. Comparison of the profiles revealed good reproducibility and a high degree of similarity among the different subjects. Of the four subjects studied, one subject had one apparent difference in the tryptic digest profile and also in the S. aureus protease V8 digest profile. The structural significance of these variations can be evaluated only after a larger number of subjects, including those presented here, have been examined; this study is now in preparation.
D001053:Apolipoproteins / Q000032:analysis*; D001055:Apolipoproteins B; D002918:Chymotrypsin; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases; D006801:Humans; D006868:Hydrolysis; D010455:Peptides / Q000302:isolation & purification; D012697:Serine Endopeptidases; D012995:Solubility; D014357:Trypsin
D001053:Apolipoproteins; D001055:Apolipoproteins B; D010455:Peptides; D010450:Endopeptidases; D012697:Serine Endopeptidases; D002918:Chymotrypsin; C028344:glutamyl endopeptidase; D014357:Trypsin