A photometric analysis of the reactions of blood coagulation

Lein, Joseph

doi:10.1002/jcp.1030300105

Cited by 8 publications

(4 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The results indicate that endotoxin does not react directly with the clottable protein (in fraction II), but apparently activates an enzyme contained in fraction I which then gels the clottable protein. Activation of fraction I by endotoxin may be analogous to the activation of prothrombin to form thrombin (15,16). The resultant enzyme(s) then reacts with the clottable protein to produce a gel, as thrombin reacts with mammalian fibrinogen to form fibrin (15,17,18).…”

Section: Discussionmentioning

confidence: 99%

“…Activation of fraction I by endotoxin may be analogous to the activation of prothrombin to form thrombin (15,16). The resultant enzyme(s) then reacts with the clottable protein to produce a gel, as thrombin reacts with mammalian fibrinogen to form fibrin (15,17,18). Endotoxin has been reported to exert effects on mammalian blood coagulation (19,20), complement (21,22), and kallekrein (23,24).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

An invertebrate coagulation system activated by endotoxin: evidence for enzymatic mediation

Young¹,

Levin²,

Prendergast³

1972

J. Clin. Invest.

182

View full text Add to dashboard Cite

A B S TRA CT Lysates prepared from the amebocytes of Limulus polyphemus, the horseshoe crab, are gelled by endotoxin. Studies were carried out to characterize the components of amebocyte lysate and to examine the kinetics of their reaction with endotoxin. Analysis of amebocyte lysate using sucrose density gradients showed two peaks at 46% and 86% gradient volumes. G50 and G75 Sephadex column chromatography resulted in three protein peaks. One fraction contained a clottable protein, which had a molecular weight of approximately 27,000, and was heat stable. Another fraction contained a high molecular weight, heat labile material, which was activated by endotoxin and reacted with the clottable protein to form a gel. The rate of the reaction between endotoxin and amebocyte lysate was dependent upon the concentration of endotoxin and the concentration of the fraction containing the high molecular weight material. The activity of this fraction was inhibited by diisopropyl fluorophosphate, parachloromercuribenzoate, and para-chloromercuriphenyl sulfonate, suggesting that enzymatic activity depended upon serine hydroxyl and sulfhydryl groups. The reaction between endotoxin and the fractions of lysate was temperature and pH dependent. The data suggest that endotoxin activates an enzyme which then gels the clottable protein contained in amebocyte lysate.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

An invertebrate coagulation system activated by endotoxin: evidence for enzymatic mediation

Young¹,

Levin²,

Prendergast³

1972

J. Clin. Invest.

182

View full text Add to dashboard Cite

show abstract

“…A variety of enzymes, including catalase, are inhibited by hydroxylamine (4)(5)(6). The effect of this substance on 'the hemolytic agent of mumps is shown in a typical experiment in Table I …”

Section: Discussionmentioning

confidence: 99%

Is Hypoprothrombinemia Caused by Deficiency of Vitamin K Different from that of Dicumarol?

Quick

Hussey

Collenthnte

1952

Experimental Biology and Medicine

View full text Add to dashboard Cite

the usual variables in bioassays by administering each form of the hormone by continuous injection. Nothing is known of the relative rates of absorption of the two forms of ACTH from the subcutaneous tissues into the blood and of their removal from the blood into the pathologic changes in the stomach and kidneys. ACTH protein had about twice the biologic activity of ACTH peptide as measured by the above criteria, but was significantly less active than the peptide in causing depletion of adrenal ascorbic acid. cells of the target organ nor is anything known about the relative proportions of the two forms of ACTH which are inactivated or otherwise wasted before they reach their target organ.The results of these experiments support the conclusion of Reinhardt and Li(1) that the bioassay of ACTH by the ascorbic acid depletion test does not always correlate with other signs of adrenal cortex response.Summary. A comparison was made of some of the metabolic and morphologic effects of ACTH protein and ACTH peptide given by continuous subcutaneous injection to normal (300 g) male rats for a period of 10 days. The signs of hypercorticalism were adrenal hyperplasia, thymus atrophy, loss in bodyweight, rise in urinary NPN, glycosuria and 1.

show abstract

“…The rigidity of the resulting clot is probably due to the cross-linking of such fibrils (7).Of considerable interest are the mechanism by which fibrinogen modification takes place, the nature of the intermediate product, and the kinetics and bonds involved in fibrin formation. Heretofore studies of reaction kinetics agreed that fibrin formation appeared to follow pseudo-first-order kinetics (6,11,13). Available evidence indicates that no extensive structural alterations take place upon fibrinogen activation or fibrin formation (1, 12, 16, 24) and thus that fibrin, just as fibrous insulin (29), represents linked corpuscular units.A technique has been developed by which the clotting reaction may be stopped quantitatively during its course and the resulting complex of nonclottable pro-…”

mentioning

confidence: 94%