PubMed · 5043149
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S Arnott, D W Hukins, J Rubin, J Brennan, M Sundaralingam. 1972-08-04. Nucleotide conformations.. https://doi.org/10.1126/science.177.4047.451
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The role of the ADP/ATP carrier (AAC), a key protein of the mitochondrial ATP-generating system, is not clear during postnatal rat heart development. To elucidate this role, the phosphorylating respiration (state 3), the activity and the content of AAC, the size of the exchangeable mitochondrial (ATP + ADP) pool and the control of AAC over respiration at state 3 were measured in mitochondria isolated from rat hearts at various postnatal ages. There was a 5-fold increase in the AAC activity from newborn to aged rat hearts, which was paralleled by a 1.5-fold increase in state 3 respiration. At birth, the AAC and the F0F1-ATP synthase exerted about 80% of the control over phosphorylating respiration (state 3: flux control coefficients 0.39 +/- 0.04 and 0.38 +/- 0.08). The strong increase in the AAC activity was partly caused by the doubling of the protein content. In addition, the turnover number of AAC increased by a factor of 2.5 due to the expansion of the (ATP + ADP) pool from 3.4 +/- 0.9 to 10.6 +/- 1.5 nmol.mg protein-1. The data strongly indicate that the increase in the AAC activity is an essential step in the postnatal maturation of rat heart mitochondria.
We examined the changes in adenosine triphosphate (ATP), lactic acid, adenosine diphosphate (ADP) and adenosine monophosphate (AMP) in five different rat muscles after death. Rigor mortis has been thought to occur simultaneously in dead muscles and hence to start in small muscles sooner than in large muscles. In this study we found that the rate of decrease in ATP was significantly different in each muscle. The greatest drop in ATP was observed in the masseter muscle. These findings contradict the conventional theory of rigor mortis. Similarly, the rates of change in ADP and lactic acid, which are thought to be related to the consumption or production of ATP, were different in each muscle. However, the rate of change of AMP was the same in each muscle.
Clusterin prepared from human serum by monoclonal antibody affinity chromatography was devoid of the ability to increase the rates of formation of insoluble immune complexes associated with clusterin preparations obtained by polyclonal IgG affinity chromatography. Clusterin did not bind to AMP-Sepharose but the protein responsible for increasing the rates of formation of insoluble immune complexes did bind to this affinity matrix. This protein was identified as complement protein C1q on the basis of its behaviour on SDS/PAGE and reactivity in sandwich ELISA with monoclonal antibodies specific for C1q. C1q (identified from its behaviour on SDS/PAGE, immunoreactivity with C1q-specific monoclonal antibodies and N-terminal sequencing data) was purified from serum by AMP-Sepharose chromatography. The binding of C1q to AMP-Sepharose was inhibited by adenine nucleotides.