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Biomedical subjects

M Foster

Publications and source records attributed to M Foster.

24 records · Page 2Linked to original sources
PubMed1977

Electron spin resonance measurements of blood caeruloplasmin and iron transferrin levels in patients with non-Hodgkin's lymphoma.

Caeruloplasmin and iron transferrin level were measured in blood of patients with non-Hodgkin's lymphoma in different stages of disease activity and compared with erythrocyte sedimentation rate and NAP level in the same samples. It was found that both caeruloplasmin level and sedimentation rate showed a slight increase in mean level in patients with active disease as compared with those in remission, particularly in the group of patients with poorly or undifferentiated diffuse disease. No difference was observed in levels of iron transferrin or NAP. Both caeruloplasmin and sedimentation rate showed occasional abnormal values in patients in remission but in most cases where both were elevated the patients subsequently entered a more active phase of the disease.

Adult↗
PubMed1975

Identification of essential arginyl residues in cytoplasmic malate dehydrogenase with butanedione.

The inactivation of cytoplasmic malate dehydrogenase (L-malate: NAD+ oxidoreductase, EC 1.1.1.37) from porcine heart and the specific modification of arginyl residues have been found to occur when the enzyme is inhibited with the reagent butanedione in sodium borate buffer. The inactivation of the enzyme was found to follow pseudo-first order kinetics. This loss of enzymatic activity was concomitant with the modification of 4 arginyl residues per molecule of enzyme. All 4 residues could be made inaccessible to modification when a malate dehydrogenase-NADH-hydroxymalonate ternary complex was formed. Only 2 of the residues were protected by NADH alone and appear to be essential. Studies of the butanedione inactivation in sodium phosphate buffer and of reactivation of enzymatic activity, upon the removal of excess butanedione and borate, support the role of borate ion stabilization in the inactivation mechanism previously reported by Riordan (Riordan, J.F. (1970) Fed. Proc. 29, Abstr. 462; Riordan, J.F. (1973) Biochemistry 12, 3915-3923). Protection from inactivation was also provided by the competitive inhibitor AMP, while nicotinamide exhibited no effect. Such results suggest that the AMP moiety of the NADH molecule is of major importance in the ability of NADH to protect the enzyme. When fluorescence titrations were used to monitor the ability of cytoplasmic malate dehydrogenase to form a binary complex with NADH and to form a ternary complex with NADH and hydroxymalonate, only the formation of ternary complex seemed to be effected by arginine modification.

Adenosine Monophosphate↗
PubMed1975

IgM paraproteins.

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Amyloidosis↗