Correcting of pronated feet reduce skeletal muscle injury in young women with biomechanical abnormalities / 대한해부학회지

Biomechanical abnormalities of pronated feet accompanied by functional leg length disparity may increase the risk of skeletal muscle injury. Objective of the study is to prove that correction of pronated feet by the foot orthoses will reduce the creatine kinase-MM (CK-MM) concentrations as the muscle injury indicator. The design study was double blind randomized clinical trials with control. Research subjects were divided into two groups, group 1 used the foot orthoses while group 2 did not used the foot orthoses. The whole subject examined the concentrations of the CK-MM enzyme before, and 24–72 hours after the walking test. The walking test was conducted 15 minutes with maximum speed. The concentration of the CK-MM enzyme before walking test on treatment group was 70.07±15.33 International Unit (IU), similar with the control group was 69.85±17.03 IU (P=0.971). The increased in CK-MM enzyme concentrations 45 hours after the walking test was lower in the treatment group (7.8±9 IU) than the control group (22.0±11.5 IU) (P=0.001). The CK-MM enzyme concentrations continued to decline in the treatment group after the second walking test (77.21±17.47 IU), and after the third walking test (69.86±11.88 IU) (P=0.018). The foot orthoses for correcting the pronated feet on the young women with biomechanical abnormalities is able to reduce the degree of the skeletal muscle injury after walking activity.

High-level expression and purification of human creatine kinase MM isozymes in E.coli / 临床检验杂志

Objective To construct a prokaryotic expression system for human creatine kinase(CK) MM isozyme,purify the recombinant protein of CK expressed in Eschericheia coli(E.coli) and examine the stability of the recombinant protein for its application in CK measurement system as the quality control.Methods Total RNA of extracted from fetal cardiac muscle was reversetranscripted and cDNA encoding human CK was amplified which was inserted into pET-15b plasmid vector.The recombinant plasmid was transfered into E.coli BL21(DE3) and induced by isopropyl-?-D-thiogalactopyranoside(IPTG).Recombinant CK-MM was separated from bacterial proteins by affinity chromatography on a Ni2+-Sepharose column.The activity of the recombinant enzyme was observed in different matrixes.Results The enzymatic activity of the crude extracts of CK-MM was up to 280,000U/L.After one step affinity chromatography,the fusion protein showed a single band in SDS-PAGE gel.The purified protein was stable and the enzymatic activity remained unchanged for a month in the matrix containing bovine serum albumin,EDTA and 1,4-Dithiothreitol(DTT).Conclusion The recombinant CK-MM showed key properties of the native creatine kinase isozyme and may be used as control and calibrator for determination of serum CK-MM.