RESUMO
Prostatic acid phosphatase and alkaline phosphatase values in bone marrow were correlated with skeletal surveys and diagnoses during a six-month study. In cases of biopsy-proven adenocarcinoma of the prostate, bone marrow prostatic acid phosphatase was the most consistently abnormal value. Diagnoses other than prostatic cancer involving the bone marrow, e.g., myeloma and leukemias, were associated with elevated prostatic acid phosphatase and alkaline phosphatase values. In cases in which the bone marrow was not involved by metastasis, these values were normal. Bone marrow prostatic acid phosphatase assay was found to be a very good tool for detecting early osseous metastases from any site, including prostatic adenocarcinoma.
Assuntos
Fosfatase Ácida/análise , Fosfatase Alcalina/análise , Medula Óssea/enzimologia , Metástase Neoplásica/diagnóstico , Adenocarcinoma/enzimologia , Neoplasias Ósseas/diagnóstico , Humanos , Leucemia/diagnóstico , Masculino , Mieloma Múltiplo/diagnóstico , Neoplasias da Próstata/enzimologiaAssuntos
Eritrócitos/metabolismo , Glicoproteínas/metabolismo , Animais , Ligação Competitiva , Bovinos , Membrana Celular/metabolismo , Centrifugação com Gradiente de Concentração , Cromatografia por Troca Iônica , Eletroforese em Gel de Poliacrilamida , Humanos , Isótopos de Iodo , Cinética , Ligação Proteica , Soroalbumina Bovina/metabolismo , Dodecilsulfato de SódioRESUMO
Mycoplasma laidlawii possesses a single glutamate dehydrogenase (GDH) with dual coenzyme specificity [specificity for nicotinamide adenine dinucleotide (H) and nicotinamide adenine dinucleotide phosphate (H)]. A purification procedure is reported which results in an enzyme preparation with a specific activity of 79.5 units/mg and which displays only one significant protein band after gel electrophoresis. This one band was determined, by activity staining, to have all of the GDH nucleotide specificities. The molecular weight of the enzyme is 250,000 +/- 10%, and it has a subunit size of about 48,000. The enzyme exhibits measurable activity with aspartate and pyruvate but is inactive with eight other possible substrates. Purine nucleotides do not affect the activity. The K(m) for reduced nicotinamide adenine dinucleotide was 1.8 x 10(-4)m. The optimal substrate concentrations and pH optimum for each of the respective GDH activities are also reported.