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Biomedical subjects

F Kanemitsu

Publications and source records attributed to F Kanemitsu.

24 records · Page 2Linked to original sources
PubMed1982

The origin of a cathode-migrating creatine kinase found in serum from a cancer patient.

The origin of an atypical creatine kinase (CK, ATP:creatine N-phosphotransferase, EC 2.7,3.2) migrating cathodic to the MM position found in the serum of a cancer patient was studied. The electrophoretic mobility of the atypical CK is similar to that of the fast-moving cathodal mitochondrial CK. The relative molecular mass was estimated to be approximately 350000, and was similar to that of the fast-moving cathodal mitochondrial CK. The atypical CK reacted with anti-human mitochondrial CK antibody. It is therefore suggested that the atypical CK is of mitochondrial origin. After incubation in 2 mol/l urea, the enzyme was converted into a new form migrating to the MM position. The conversion was observed in liver mitochondrial CK but not heart mitochondrial CK. The residual CK activity after heating at 56 degrees C for 60 s was 77%, and the apparent Km value for creatine phosphate at 30 degrees C was about 0.27 mmol for the atypical CK. These characteristics were very similar to those of the liver mitochondrial CK, because the data from the enzyme determined at the same time were 75% for residual enzyme activity to heat, and 0.24 mmol for apparent Km value. Therefore liver mitochondria are suggested to be the source of the atypical CK.

Adult↗
PubMed1982

Characteristics of mitochondrial creatine kinases from normal human heart and liver tissues.

Mitochondrial creatine kinases (CKs, ATP:creatine N-phosphotransferases, EC 2.7.3.2) were isolated from normal human heart and liver, and their characteristics were compared. The electrophoretic patterns of the extracted enzymes exhibited two forms both migrating cathodic to CK-MM. The fast-moving cathodal form is the major form and the slow-moving cathodal form is the minor one. Incubation of the heart mitochondrial CK at 37 degrees C in normal human serum for 7 h and of the liver mitochondrial CK at 26 degrees C for 1 h in 2 mol/l urea, converted the fast-moving form into the slow-moving one, and finally into a third form migrating in the MM position. The relative molecular masses were estimated to be approximately 350,000 for the major form, and 80,000 for the minor and the third forms. The electrophoretic mobility and molecular weight of the third form were identical to those of the CK-MM; however, the third form was distinguished from CK-MM by its different antigenicity. Thus, three forms were ultimately recognized as mitochondrial CKs by electrophoretic mobilities and molecular weights. The liver mitochondrial CK reacted with anti-human heart mitochondrial CK antibody, thus these two isoenzymes could not be discriminated by their antigenicities. The liver mitochondrial CK was more stable to heat and had higher apparent affinity for creatine phosphate than the heart mitochondrial CK.

Antibody Formation↗
PubMed1981

Three atypical serum creatine kinases in a patient with carcinoma of the colon.

Three electrophoretically atypical creatine kinase (CK) bands were found simultaneously in the serum of a patient with terminal carcinoma of the colon. The atypical CKs were found at the cathodal side of CK-MB (CK-X1), at a sample application point (CK-X2), and at the anodal side of CK-MM (CK-X3) on agar plates. Our data seemed to suggest that CK-X1 was predominantly a CK-IgA/beta-lipoprotein complex, CK-X3 was a CK-IgG complex, and CK-X2 was macromolecular, different from both CK-X1 and CK-X3. The light chains of IgA and IgG were both of the lambda type. All native isoenzymes comprising these atypical CKs were identified as MM type. There was no change of the electrophoretic pattern of serum CK isoenzymes throughout the course of the study.

Aged↗