## Abstract Porcine pancreatic phospholipase A~2~ was purified from commercial pancreatin by a method involving heat denaturation, trichloroacetic acid precipitation, and DEAE‐cellulose chromatography. Assaying the eluate of the chromatography step by a new titrimetric method using vegetable lecith
Multiple forms of porcine pancreatic α-amylase
✍ Scribed by J.Julian M. Rowe; Jubran Wakim; John A. Thoma
- Publisher
- Elsevier Science
- Year
- 1968
- Tongue
- English
- Weight
- 829 KB
- Volume
- 25
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
The catalytic efficiency (kcat/K m) and the cleaved bond distribution for the nitrophenylated maltooligosaccharides, p-NPGlc n (2 ~ n ~< 7) hydrolysed by porcine pancreatic alpha-amylase isozymes I and II were determined. The subsite affinities (A i) were calculated from the p-NPGIc n (4 ~< n ~< 7)
The effect of the oligosaccharide analog maltotriitol (G3OH) on the action pattern of porcine pancreatic alpha-amylase (PPA) was examined using amylose as a substrate. Fluorescence titration indicated that two molecules of G3OH can bind to one molecule of PPA. The slope in the blue value versus exte