Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0267964 (PAA)
 2,561 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The role of macrophages in the in vitro response of mouse spleen cells to the insolubilized, T-independent antigen trinitrophenylated polyacrylamide (TNP-PAA) is demonstrated by the following points. The response is abolished by filtration on Sephadex G-10 and can be restored by the addition of splenic adherent cells, deficient in either B or T cells, or by 2-mercaptoethanol (2ME). It is suppressed upon elimination of phagocytic cells by silica, and restored by 2-ME. 2-ME can restore a normal response from zero, in cultures depleted of both adherent and phagocytic cells, and is efficient in the absence of mature T cells. Experiments in microcultures show that large numbers of macrophages can stimulate a supra-optimal response from B cells. This response is only obtained in the presence of the antigen, and is specific for TNP. These results show that microphages, probably by their polyclonal B-cell activator (PBA) property, play a role in the specific response to TNP-PAA. This prompts us to discuss the respective roles in the B-cell response of this PBA activity and of the interaction of the antigen with the specific B-cell receptors.
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PMID:Macrophage requirement for the in vitro response to an insolubilized T-independent antigen. 31 10

A method is described wherein blood samples taken from adults or newborns and dried on filter paper can be used for hemoglobin analysis within 2 years after sampling. The samples are eluted in 8 M urea in the presence of 5% 2-mercaptoethanol and 2% of the neutral detergent Nonidet P-40. Then the individual alpha, beta, gamma, and epsilon chains are separated by means of electrofocusing in 8 M urea-PAA gels. Up to 96 samples can be applied to a gel using multiple syringes. Several hundred samples can be analyzed daily by one person. This method may be especially useful for preventive programs against sickle cell anemia as well as for human mutation monitoring systems.
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PMID:Improved screening test for abnormal hemoglobins from dried blood samples. 53 5

The substrate that was split most rapidly by acid phosphatase was p-nitrophenylphosphate. Two peaks of activity were obtained at pH 4.6-4.8 and 5.1-5.4. The enzyme remained stable for a long time when refrigerated. It was inhibited strongly by urea and tartrate, and slightly by fluoride and L-phenylalanine. Mercaptoethanol elicited pronounced activation of the enzyme. Four different forms of isoenzyme, giving rise to 11 phenotypes, were identified. A suitable analytical technique was electrophoresis on polyacrylamide gel with phosphate-citrate buffer. Mean activity was 3.15 +/- 0.41 units per gramme of haemoglobin haemolysate. Some of the isoenzyme preparations showed considerable variation in activity. There was no change in enzyme activity after temporary hypomagnesaemia. Acid phosphatase activity was high in testis, kidney and intestinal mucosa; myocardium, liver and spleen showed moderate activity. Five isoenzymes were demonstrable in a starch column and six in PAA gel.
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PMID:[Properties and isoenzymes of acid phosphatase in erythrocytes and various tissues (kidney, liver, spleen, small intestine mucosa, testis, myocardial and skeletal musculature) of cattle]. 122 26