THE ASSOCIATION OF LIPOPROTEINS WITH THE INHIBITION OF STREPTOLYSIN-S BY SERUM
THE ASSOCIATION OF LIPOPROTEINS WITH THE INHIBITION OF STREPTOLYSIN-S BY SERUM
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DOI:
10.1172/jci102408
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发表时间:
1950-01-01
影响因子:
15.9
通讯作者:
MACLEOD, CM
中科院分区:
文献类型:
--
作者:
STOLLERMAN, GH;BERNHEIMER, AW;MACLEOD, CM
The inhibition of streptolysin S is due to normal components of serum rather than to a specific antibody. The sera of a wide variety of normal animal spp. inhibit streptolysin S and this inhibition is independent of gamma globulins in the sera of humans, rabbits and horses. Specific antibodies to streptolysin S did not appear when rabbits were injd. with streptolysin S or with live cultures of beta-hemolytic streptococci. The highest degree of strepto-lysin S inhibition appears in the serum fractions associated with alpha-1 and beta-1 lipoproteins when serum is fractionated by the cold alcohol method. When serum is fractionated by salting out with ammonium sulfate, the albumin fraction is also associated with streptolysin S inhibition. Saline suspensions of phospholipids, particularly lecithin, inhibit streptolysin S. A marked reduction of streptolysin S inhibition occurs when serum is treated with Clostridium welchii lecithinase, or with ether or ether-alcohol mixture. Inhibition of streptolysin S by serum is increased by tryptic digestion, by heating near the coagulation point, by prolonged storage at or above 4[degree]C, and by fractionation with ammonium sulfate. Following fractionation with ammonium sulfate, the increase in total inhibitory activity of horse serum was 3.75 times, and of human serum 2.41 times. In each instance, treatment with lecithinase or with ether produces a marked decrease in streptolysin S inhibition. The streptolysin S inhibitor in serum appears to be composed of a phospholipo-protein complex and the phospholipids of serum may play a role in its stabilization as well as in its composition.