Proteinase Inhibitor Gene Families: Tissue Specificity and Regulation
Proteinase Inhibitor Gene Families: Tissue Specificity and Regulation
复制标题
蛋白酶抑制剂基因家族:组织特异性和调控
DOI:
10.1007/978-3-7091-6950-6_12
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发表时间:
1988
影响因子:
6.4
通讯作者:
C. Ryan
中科院分区:
文献类型:
--
作者:
C. Ryan
Proteinase inhibtors are a multifamily group of proteins that are ubiquitous in nature (Laskowski, Jr. and Kato, 1984). Inhibitor proteins have been isolated that specifically inhibit each of the four known mechanistic classes of proteolytic enzymes, i. e. serine, thiol, aspartyl and metalloproteinases. Overall, the serine proteinase inhibitors comprise over ten unrelated protein families (Laskowski, Jr., 1986) that are found within the animal and plant kingdoms (Table 1). The functional role of these inhibitor proteins appears to be either to protect tissues or fluids from proteolysis by foreign proteases or to regulate the levels of proteases that are metabolically active in the tissues or fluids that they are associated with. The majority of proteinase inhibitor proteins that have been purified from plants have been inhibitors of serine endopeptidases such as the animal digestive enzymes trypsin, chymotrypsin and elastase or the bacterial proteinase subtilisin. In plants, the inhibitor proteins usually account for from 1 – 15 % or more of the proteins of various storage organs such as seeds and tubers (Ryan, 1974) and in some plant species, in leaves, in fruit, or in both (see below).
DOI:
10.1073/pnas.83.19.7277
发表时间:
1986-10-01
影响因子:
11.1
作者:
LEE, JS;BROWN, WE;RYAN, CA
通讯作者:
RYAN, CA