Angiotensin I-Converting Enzyme Inhibitory Substances in Black Matpe.

Accession number;99A0562724
Title;Angiotensin I-Converting Enzyme Inhibitory Substances in Black Matpe.
Author; YOSHIDA KEIKO (Tsukubakokusaitandai) TSURUSHIIN SHIGEKO (Tokyo Kasei Gakuin Jr. Coll.) FUKUBA HIROYASU (Showa Women's Univ.) SHIMAMURA RIMIKO (Tokyo Univ. Agriculture, Dep. Applied Biology and Chemistry, JPN) TADOKORO TADAHIRO (Tokyo Univ. Agriculture, Dep. Applied Biology and Chemistry, JPN) MAEKAWA AKIO (Tokyo Univ. Agriculture, Dep. Applied Biology and Chemistry, JPN)
Journal Title;Journal of Japanese Society of Nutrition and Food Science
Journal Code:F0624A
ISSN:0287-3516
VOL.52;NO.3;PAGE.153-156(1999)
Figure&Table&Reference;FIG.4, REF.17
Pub. Country;Japan
Language;Japanese
Abstract;ACE inhibitory substances in black matpe constituted a hydrophilic group with a molecular weight of about 400-800, estimated by gel filtration on a Sephadex G-15 column. These inhibitory substances could not be separated using reverse-phase HPLC, gel filtration or ion exchange columns. The ACE inhibitory substances contained phylic acid, which when extracted had 40% of the total activity. When the ACE inhibitory substances were analyzed by TLC, some ninhydrin-positive spots were observed, whereas the phyiic acid fraction contained no ninhydrin-positive spots. These results suggest that the substances are a mixture of phytic acid and ninhydrin-positive material. (author abst.)
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