Feldmann K, Zeisel H, Helmreich E
Proc Natl Acad Sci U S A. 1972 Aug;69(8):2278-82. doi: 10.1073/pnas.69.8.2278.
Phospho-dephosphohybrids of rabbit skeletal muscle phosphorylase (EC 2.4.1.1; alpha-1,4-glucan: orthophosphate glucosyl transferase) have been prepared and stabilized by attachment to Sepharose activated by cyanogen bromide. They can be distinguished from phosphorylase a by their sensitivity to inhibition by glucose-6-phosphate and activation by adenosine 5'-monophosphate. Stable hybrids have also been formed between phosphorylase subunits containing the active cofactor pyridoxal-phosphate and inactive analogs (pyridoxalphosphate monomethylester or the corresponding reduced compounds). After complete dissociation to monomers, the Sepharose-bound phosphorylase had a residual activity of less than 3% of that of the original matrix-bound dimeric enzyme. The hybrid enzyme is composed of a potentially active subunit containing pyridoxal-phosphate and an intrinsically inactive subunit carrying the analog, and it had half the activity of the original dimeric enzyme. Thus, the interaction of the inactive subunit with matrix-bound phosphorylase monomers elicited activity in the monomers.
兔骨骼肌磷酸化酶（EC 2.4.1.1；α-1,4-葡聚糖：正磷酸葡萄糖基转移酶）的磷酸化-去磷酸化杂种已制备出来，并通过与溴化氰活化的琼脂糖结合而得以稳定。它们可通过对6-磷酸葡萄糖抑制的敏感性和对5'-单磷酸腺苷激活的敏感性与磷酸化酶a区分开来。在含有活性辅因子磷酸吡哆醛的磷酸化酶亚基与无活性类似物（磷酸吡哆醛单甲酯或相应的还原化合物）之间也形成了稳定的杂种。完全解离为单体后，与琼脂糖结合的磷酸化酶的残余活性不到原始与基质结合的二聚体酶活性的3%。杂种酶由一个含有磷酸吡哆醛的潜在活性亚基和一个携带类似物的内在无活性亚基组成，其活性为原始二聚体酶的一半。因此，无活性亚基与与基质结合的磷酸化酶单体的相互作用引发了单体中的活性。
