PRESERVATION OF METABOLIC-ACTIVITY IN LYOPHILIZED HUMAN ERYTHROCYTES
PRESERVATION OF METABOLIC-ACTIVITY IN LYOPHILIZED HUMAN ERYTHROCYTES
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DOI：
10.1073/pnas.89.3.967
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发表时间：
1992-02-01
影响因子：
11.1
通讯作者：
TANAKA, KR
中科院分区：
文献类型：
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作者：
GOODRICH, RP;SOWEMIMOCOKER, SO;TANAKA, KR
正常人红细胞（RBC）在引起正常RBC代谢活性最小改变的条件下冷冻干燥。由于已知长期储存对代谢活性的影响，我们研究了冻干工艺对RBC代谢的影响。在研究的所有代谢酶中，与新鲜对照非冻干RBC相比，仅磷酸丙糖异构酶（D-甘油醛-3-磷酸酮醇异构酶，EC 5.3.1.1）、烯醇酶（2-磷酸-D-甘油酸水解酶，EC 4.2.1.11）和丙酮酸激酶（ATP：丙酮酸O2-磷酸转移酶，EC 2.7.1.40）降低。这些酶的活性与血库RBC的活性无显著差异。在冻干红细胞中，高能中间体ATP和2，3-二磷酸甘油酸的浓度以及乳酸和ATP的产生沿着降低。在冻干过程中，磷酸戊糖分流的酶没有改变。此外，我们的数据表明，冻干红细胞具有完整的能力（i）合成腺嘌呤核苷酸和（ii）减少甲基血红蛋白，从而保持血红蛋白在一个功能性的生理状态类似于新鲜的非冻干红细胞。 目前的研究表明，冻干红细胞的方式，保持正常的代谢和酶功能后，再水化的可能性。
Normal human erythrocytes (RBC) were freeze-dried under conditions that caused minimal modification in normal RBC metabolic activities. Because of the known effects of long-term storage on metabolic activities, we studied the effects of our lyophilization process on RBC metabolism. Of all the metabolic enzymes studied, only triosephosphate isomerase (D-glyceraldehyde-3-phosphate ketol-isomerase, EC 5.3.1.1), enolase (2-phospho-D-glyceratehydro-lyase, EC 4.2.1.11), and pyruvate kinase (ATP:pyruvate O2-phospho-transferase, EC 2.7.1.40) were decreased when compared with fresh control nonlyophilized RBC. The activities of these enzymes did not differ significantly from those of blood bank RBC. Concentrations of high-energy intermediates, ATP, and 2,3-diphosphoglycerate, along with lactate and ATP production were decreased in lyophilized RBC. No enzymes of the pentose phosphate shunt were altered during lyophilization. In addition, our data show that lyophilized RBC possess an intact capacity to (i) synthesize adenine nucleotides and (ii) reduce Meth to Hb and, thus, maintain the Hb in a functional physiologic state similar to fresh nonlyophilized RBC. The present study demonstrates the possibility of lyophilizing RBC in a manner that maintains normal metabolic and enzymatic function upon rehydration.