Reference

In vivo and in vitro effects of thrombin and plasmin on human factor VIII (AHF)

In vivo and in vitro effects of thrombin and plasmin on human factor VIII (AHF). Lian, Eric C.; Nunez, Roger L.; Harkness, Donald R. (Dep. Med., VA Hosp., Miami, Fla., USA). Am. J. Hematol., 1(4), 481-91 (English) 1976. CODEN: AJHEDD. DOCUMENT TYPE: Journal CA Section: 1 (Pharmacodynamics) Section cross-reference(s): 14 The relationship between factor VIII [9001-27-8] procoagulant activity and factor VIII-related antigen were examd. in patients with disseminated intravascular coagulation (DIC), pulmonary embolism (PE), and coronary artery disease with or without myocardial infarction (MI). 9001-27-8 and 9001-90-5 are cas registry numbers of chemicals which are used as reagents here. Thirteen of 13 patients with DIC, 17 of 17 patients with PE, and 10 of 12 patients with MI possessed a significantly elevated factor VIII-related antigen to factor VIII activity ratio (VIII-ratio). The VIII-ratio returned to normal in each of 2 patients with DIC and 1 patient with PE after treatment with heparin [9005-49-6], heparin and .alpha.-aminocaproic acid [327-57-1], and heparin and coumadin [81-81-2] resp. In contrast, the VIII-ratio was slightly elevated only in 1 of 15 patients with coronary artery insufficiency without MI. In vitro, after treatment of plasma with thrombin [9002-04-4] or plasmin [9001-90-5], factor VIII activity was lost, whereas the amt. of factor VIII-related antigen remained the same or was even increased when measured by agarose quant. immunoelectrophoresis. Thus, an elevated VIII-ratio is a very sensitive indicator of intravascular coagulation. .

Presynaptic binding of amino acids: characterization of the binding and dissociation properties of taurine, GABA, glutamate, tyrosine and norleucine

Presynaptic binding of amino acids: characterization of the binding and dissociation properties of taurine, GABA, glutamate, tyrosine and norleucine. Turpeenoja, Leena; Lahdesmaki, P. (Dep. Biochem., Univ. Oulu, Oulu SF-90570/57, Finland). Int. J. Neurosci., 22(1-2), 99-106 (English) 1983. CODEN: IJNUB7. ISSN: 0020-7454. DOCUMENT TYPE: Journal CA Section: 2 (Mammalian Hormones) Section cross-reference(s): 6, 9 Calf brain synaptic plasma membranes (SPM) were satd. under extracellular conditions with the 14C-labeled compds. glutamic acid [56-86-0], GABA [56-12-2], taurine [107-35-7], or norleucine [327-57-1] or 3H-labeled tyrosine [60-18-4], and the resulting labeled membrane complexes were fractionated by a differential extn. procedure using 0.9% NaCl, distd. water, n-BuOH-water, 0.05M NaOH, and 0.5% Triton X-100 [9002-93-1] solns., in this order. Free and protein-bound radioactivities were measured in the exts. Glutamate had the highest and taurine the lowest affinity of binding to the original membranes, the ratios of bound/free label being 1/40 for glutamate, ~1/200 for GABA and norleucine, 1/673 for tyrosine, and 1/1447 for taurine. The molar binding capacities were lowest for tyrosine and highest for glutamate.Several substances with their cas registry numbers 107-35-7 and 7732-18-5 may be metioned in this study. About 2/3 of the proteins of SPM could be solubilized, and 1/3 of them remained insol. after use of the above series of extns. Triton X-100 was the most effective solubilizer, liberating ~24% of the membrane proteins, but only 4-7% of the label. Distd. water solubilized ~15%, 0.9% NaCl 10%, and 0.05M NaOH also 10% of the proteins. NaOH was the most potent solubilizer for the protein-bound label (50-70%), even though it was used in the 4th position in the series. On the other hand, 0.9% NaCl and distd. water extd. the mostly loosely-bound radioactivity from SPM. Apparently, GABA and norleucine, in general, were most easily dissocd., and taurine, tyrosine, and glutamate had the highest affinity for assocn. with the protein fractions of SPM. .