Stenman U H
Scand J Clin Lab Invest. 1975 Mar;35(2):147-55. doi: 10.1080/00365517509087218.
The R-type vitamin B12-binding proteins, here called cobalophilin, in human plasma, serum, leukocytes, gastric juice, amniotic fluid, and milk, were characterized by isoelectric focusing and gel filtration. Cobalophilin from all these sources in microheterogenous, consisting of several isoproteins with isoelectric points (pI) between 2.3 and 5.0. Isoproteins with pI values of 3.0, 3.3, 3.6, 3.9, and 4.2 were found in most of the cells and fluids studied, but in different proportions. Milk contains isoproteins with pI values mainly between 4.0 and 4.7, and such components also occur in considerable amounts in saliva. The cobalophilin in these fluids also has a smaller Stokes radius than that from other sources. On the basis of the isoelectric patterns and the Stokes radii the isoproteins of cobalophilin are tentatively divided into two populations, a glandular one occurring in milk and saliva and a myelogenic one occurring in all the cells and fluids studied but only occasionally in milk.
人血浆、血清、白细胞、胃液、羊水和乳汁中的R型维生素B₁₂结合蛋白，在此称为钴胺素结合蛋白，通过等电聚焦和凝胶过滤进行了表征。来自所有这些来源的钴胺素结合蛋白是微异质的，由几种等电点（pI）在2.3至5.0之间的同功蛋白组成。在大多数研究的细胞和液体中发现了等电点值为3.0、3.3、3.6、3.9和4.2的同功蛋白，但比例不同。乳汁中含有的同功蛋白等电点值主要在4.0至4.7之间，并且这些成分在唾液中也大量存在。这些液体中的钴胺素结合蛋白的斯托克斯半径也比其他来源的小。根据等电模式和斯托克斯半径，钴胺素结合蛋白的同功蛋白初步分为两类，一类是存在于乳汁和唾液中的腺源性同功蛋白，另一类是存在于所有研究的细胞和液体中但仅偶尔存在于乳汁中的骨髓源性同功蛋白。
