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H Nishimaki

Publications and source records attributed to H Nishimaki.

31 records · Page 2Linked to original sources
PubMed1992

[Clinical evaluation of hepatic scintigraphy using 99mTc-GSA].

Functional hepatic imaging was performed using 99mTc-DTPA-galactosyl human serum albumin (99mTc-GSA), a radiolabeled ligand that reacts specifically to the asialoglycoprotein receptor that resides at the plasma membrane of hepatocytes, in 21 patients: five with chronic active hepatitis (CAH), 14 with compensative liver cirrhosis (LC), one with chronic inactive hepatitis and one with acute hepatitis. The former two diseases were mainly investigated. Serial liver images were acquired at the rates of 10 sec/frame for 0-5 min and 2 min/frame for 6-30 min after the injection of 99mTc-GSA, and the images were compared with 99mTc-phytate images in 2 patients with CAH and 11 with LC, and those with portal scintigrams using 123I-iodoamphetamine (IMP) in 3 patients with LC. The images using 99mTc-GSA were in better agreement with hepatic function than those using 99mTc-phytate, and with the findings of portal scintigraphy using 123I-IMP. LHL15 (liver/liver and heart radioactivities at 15 min after the injection of 99mTc-GSA) correlated with the hepaplastin test (r = 0.978 in CAH, and r = 0.544 in LC), indicators of hepatic reserve. These results suggest that liver scintigraphy using 99mTc-GSA might be a useful method for evaluating liver function.

Adult↗
PubMed1990

[Clinical evaluation of renoscintigraphy using 123I-orthoiodohippurate--comparison with 131I-OIH and measurement of the effective renal blood flow].

Renoscintigraphy using 123I-orthoiodohipprate (123I-OIH) was conducted, and the dynamic imaging study results and the renograms were analyzed. The results using 123I-OIH were compared with those using 131I-OIH in 22 of 33 patients. Measurement of the effective renal blood flow (ERBF) was also performed using 123I-OIH by the single blood-sample method. 123I is a more suitable nuclide for gamma-camera scintigraphy than 131I in terms of physical characteristics, and a larger dose of 123I-OIH is possible than 131I-OIH because of its lesser radiation. These are the reasons why clearer dynamic images of the blood flow phase, functional phase and excretion phase can be obtained. These make possible diagnoses associated with the organic changes and functions. No essential differences could be found in the functional study results of renogram between the two drugs because on the nuclide of 131I is replaced by 123I, but a renogram with less statistical noise could be obtained using 123I-OIH than 131I-OIH. The radiation dose of 123I-OIH is less than that of 131I-OHI, and clearer dynamic images and functional indexes can be easily obtained in scintigraphy using 123I-OIH. It is concluded that 123I-OIH is a useful radiopharmaceutical for renal examination, and it should replace 131I-OIH.

Adolescent↗
PubMed1987

Purification and characterization of human liver branched-chain alpha-keto acid dehydrogenase complex.

Human liver BCKADH complex was purified. On SDS-polyacrylamide gel electrophoresis, the purified enzyme complex gave three major bands having molecular weights of 51,000, 46,000, and 36,000, and one minor band with a molecular weight of 55,000. The minor band corresponded in molecular weight to lipoamide oxidoreductase which was purified separately. The purified BCKADH represented only approximately 20% of the maximum activity when assayed without addition of exogenous lipoamide oxidoreductase, indicating that lipoamide oxidoreductase component was readily dissociable from the complex. The BCKADH effectively oxidized all of KIV, KIC, and KMV, yielding apparent Km values in the range of 14-17 microM for those alpha-keto acids. Vmax values obtained were 0.86, 0.61, and 0.51 mumole NADH produced/min/mg of protein for KIV, KIC, and KMV, respectively, in the presence of excess amount of lipoamide oxidoreductase. This ratio of Vmax values was practically identical to those of specific activities obtained with respective branched-chain alpha-keto acids at each purification step. The enzyme complex also oxidized pyruvate and alpha-ketoglutarate to a lesser extent. Kinetic experiments gave Km values of 0.98 and 2.9 mM for pyruvate and alpha-ketoglutarate, respectively, with Vmax of 0.43 and 0.08 mumole NADH produced/min/mg of protein. NAD and CoASH were absolutely required for the reaction. Km values for NAD and CoASH were estimated to be 47 and 25 microM, respectively.

3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)↗