阿拉伯单峰骆驼（骆驼属单峰驼）肝脏磷酸果糖激酶的纯化、特性及调节特性

The purification, characterization and regulatory properties of liver phosphofructokinase in the Arabian one-humped camel (Camelus dromedarius).

Khoja S M, Rizk A M, Abulgasim A O

Comp Biochem Physiol B. 1987;87(2):335-40. doi: 10.1016/0305-0491(87)90148-9.

Abstract

Phosphofructokinase from camel liver was purified to homogeneity more than 3600-fold, and the yield of the preparation was 46%. 2. The sodium dodecyl sulphate-treated purified enzyme migrated as a single band in 10% polyacrylamide gel. 3. The enzyme is a tetramer, with a monomer Mr 90,000. 4. The regulatory properties of the purified enzyme from camel liver were studied at pH 7.0. 5. The enzyme displayed cooperativity with respect to fructose 6-phosphate and was inhibited by high concentrations of ATP. 6. The enzyme was also inhibited by citrate, phosphocreatine and 2,3-bisphosphoglycerate. 7. On the other hand, ADP, AMP, glucose 1,6-bisphosphate and fructose 2,6-bisphosphate were all found to be strong activators for camel liver phosphofructokinase.

摘要

骆驼肝脏中的磷酸果糖激酶被纯化至均一性，纯化倍数超过3600倍，制剂产率为46%。2. 经十二烷基硫酸钠处理的纯化酶在10%聚丙烯酰胺凝胶中迁移为单一条带。3. 该酶是一种四聚体，单体分子量为90,000。4. 在pH 7.0条件下研究了骆驼肝脏纯化酶的调节特性。5. 该酶对6-磷酸果糖表现出协同性，并受到高浓度ATP的抑制。6. 该酶也受到柠檬酸、磷酸肌酸和2,3-二磷酸甘油酸的抑制。7. 另一方面，发现ADP、AMP、1,6-二磷酸葡萄糖和2,6-二磷酸果糖都是骆驼肝脏磷酸果糖激酶的强激活剂。