Tate S S, Khadse V
Biochem Biophys Res Commun. 1986 Dec 30;141(3):1189-94. doi: 10.1016/s0006-291x(86)80170-x.
The molecular weights (Mr) of mammalian renal gamma-glutamyl transpeptidase light subunits vary from 21 to 25 K; a much broader range is seen for the large subunit (51 to 72 K). However, chemical deglycosylation of these enzymes (rat, human, and bovine) yields subunits each of which exhibits identical Mr (41 and 19 K for the heavy and light subunits, respectively), suggesting strong similarity between the peptide backbones of these glycoproteins. Immunological data also indicate homologies between these enzymes. The difference observed in the Mr of native subunits thus seem to be related to the extent and nature of glycosylation of these proteins.
哺乳动物肾脏γ-谷氨酰转肽酶轻亚基的分子量（Mr）在21至25千道尔顿之间变化；大亚基的分子量范围则宽得多（51至72千道尔顿）。然而，对这些酶（大鼠、人类和牛的）进行化学去糖基化处理后，每个亚基都呈现出相同的分子量（重亚基和轻亚基分别为41和19千道尔顿），这表明这些糖蛋白的肽主链之间具有很强的相似性。免疫学数据也表明这些酶之间存在同源性。因此，天然亚基分子量的差异似乎与这些蛋白质的糖基化程度和性质有关。
