Isolation and characterization from potato tubers of two polypeptide inhibitors of serine proteinases.
Isolation and characterization from potato tubers of two polypeptide inhibitors of serine proteinases.
复制标题
从马铃薯块茎中分离和鉴定两种丝氨酸蛋白酶多肽抑制剂。
DOI:
10.1016/0003-9861(82)90571-9
复制
发表时间:
1982
影响因子:
3.9
通讯作者:
G. Hass
中科院分区:
文献类型:
--
作者:
G. Pearce;L. Sy;C. Russell;C. Ryan;G. Hass
Two polypeptides, isolated to electrophoretic homogeneity from Russet Burbank potato tubers, are powerful inhibitors of pancreatic serine proteinases. One of the inhibitors, called polypeptide trypsin inhibitor, PTI, has a molecular weight of 5100, and inhibits bovine trypsin. The inhibitor is devoid of methionine, histidine, and tryptophan and contains eight half-cystine residues as four disulfide bridges. The second inhibitor, polypeptide chymotrypsin inhibitor II, PCI-II, has a molecular weight of 5700 and powerfully inhibits chymotrypsin. This inhibitor is also devoid of methionine and tryptophan but it contains only six of half-cystines as three disulflde bonds. Both polypeptides strongly inhibit pancreatic elastase. In immunological double diffusion assays, polypeptide trypsin inhibitor and polypeptide chymotrypsin inhibitor II exhibit a high degree of immunological identity (a) with each other, (b) with a polypeptide chymotrypsin inhibitor (PCI-I,Mr5400) previously isolated from potato tubers, and (c) with inhibitor II, a larger (monomerMr~ 12,000) inhibitor of both trypsin and chymotrypsin which has also been previously isolated from potato tubers. The four polypeptide proteinase inhibitors now isolated from Russet Burbank potato tubers cumulatively inhibit all five major intestinal digestive endo- and exoproteinases of animals. The inhibitors are thought to be antinutrients that are present as part of the natural chemical defense mechanisms of potato tubers against attacking pests.