Albersheim P, Anderson A J
Proc Natl Acad Sci U S A. 1971 Aug;68(8):1815-9. doi: 10.1073/pnas.68.8.1815.
Proteins extracted from the cell walls of Red Kidney bean hypocotyls, tomato stems, and suspension-cultured sycamore cells can completely inhibit the activity of the polygalacturonases (polygalacturonide hydrolases, EC 3.2.1.15) secreted by the fungal plant pathogens Colletotrichum lindemuthianum, Fusarium oxysporum, and Sclerotium rolfsii. The inhibitor of the C. lindemuthianum polygalacturonase, purified 560-fold from bean hypocotyl extracts, is 40 times as effective an inhibitor of the C. lindemuthianum polygalacturonase as of the F. oxysporum polygalacturonase, and does not demonstrably inhibit the S. rolfsii polygalacturonase. A crude hypocotyl extract that completely inhibits the three polygalacturonases does not inhibit C. lindemuthianum-secreted cellulase, xylanase, alpha-galactosidase, alpha-arabinofuranosidase, or alpha-galacturonosidase. The purified bean hypocotyl protein combines with the C. lindemuthianum polygalacturonase to form a complex with a dissociation constant of 2 x 10(-9) M or less. The physical properties of these inhibitors are similar to those of phytohemagglutinins and of the plant glycoproteins capable of agglutinating transformed animal cells.
从红芸豆下胚轴、番茄茎以及悬浮培养的悬铃木细胞的细胞壁中提取的蛋白质，能够完全抑制由植物病原真菌菜豆炭疽菌、尖孢镰刀菌和齐整小核菌分泌的多聚半乳糖醛酸酶（多聚半乳糖醛酸水解酶，EC 3.2.1.15）的活性。从菜豆下胚轴提取物中纯化560倍得到的菜豆炭疽菌多聚半乳糖醛酸酶抑制剂，对菜豆炭疽菌多聚半乳糖醛酸酶的抑制效果是对尖孢镰刀菌多聚半乳糖醛酸酶抑制效果的40倍，并且对齐整小核菌多聚半乳糖醛酸酶没有明显抑制作用。一种能完全抑制这三种多聚半乳糖醛酸酶的粗制下胚轴提取物，不会抑制菜豆炭疽菌分泌的纤维素酶、木聚糖酶、α-半乳糖苷酶、α-阿拉伯呋喃糖苷酶或α-半乳糖醛酸苷酶。纯化后的菜豆下胚轴蛋白与菜豆炭疽菌多聚半乳糖醛酸酶结合形成一种解离常数为2×10⁻⁹ M或更低的复合物。这些抑制剂的物理性质与植物血凝素以及能够凝集转化动物细胞的植物糖蛋白的物理性质相似。
