Nicholson B J, Takemoto L J, Hunkapiller M W, Hood L E, Revel J P
Cell. 1983 Mar;32(3):967-78. doi: 10.1016/0092-8674(83)90081-8.
Liver gap junctions and gap-junction-like structures from eye lenses are each comprised of a single major protein (Mr 28,000 and 26,000, respectively). These proteins display different two-dimensional peptide fingerprints, distinct amino acid compositions, nonhomologous N-terminal amino acid sequences and different sensitivities to proteases when part of the intact junction. However, the junctional protein of each tissue is well conserved between species, as demonstrated previously for lens and now for liver in several mammalian species. The possiblity of tissue-specific gap junction proteins is discussed in the light of data suggesting that rat heart gap junctions are comprised of yet a third protein.
肝组织中的间隙连接以及晶状体中类似间隙连接的结构,各自均由单一主要蛋白质构成(分子量分别为28,000和26,000)。这些蛋白质呈现出不同的二维肽指纹图谱、各异的氨基酸组成、非同源的N端氨基酸序列,并且在完整连接结构中时对蛋白酶的敏感性也不同。然而,正如先前在晶状体中所证实的以及现在在几种哺乳动物肝脏中所证实的那样,每个组织的连接蛋白在物种间具有高度保守性。鉴于有数据表明大鼠心脏间隙连接由第三种蛋白质构成,因此对组织特异性间隙连接蛋白的可能性进行了讨论。