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Coagulation protein function. II. Influence of thiols upon acetaldehyde effects
A P Koterba1, S Smolen, A Joseph
1Department of Biological Sciences, Bowling Green State University, OH 43403, USA.
Alcohol (Fayetteville, N.Y.)
|January 1, 1995
Summary
Acetaldehyde (AcH) prolongs clotting time by interacting with clotting proteins. Certain amino acids and dithiothreitol (DTT) also affect clotting, with some potentially mitigating AcH
Area of Science:
- Biochemistry
- Hematology
Background:
- Acetaldehyde (AcH) can prolong prothrombin time by alkylating clotting proteins.
- Understanding interactions between AcH and plasma components is crucial for hematological studies.
Purpose of the Study:
- To investigate the effects of various compounds on blood clotting time.
- To examine the interaction of these compounds with acetaldehyde (AcH).
Main Methods:
- Assessing clotting time in plasma after incubation with L-cysteine (CysH), DL-homocysteine (HC), D-penicillamine, N-acetyl-L-cysteine (NAC), L-serine, L-alanine, lactalbumin hydrolysate, and dithiothreitol (DTT).
- Evaluating the impact of pre-incubation and sequential addition of AcH and other compounds on clotting.
- Analyzing potential adduct formation between AcH and test compounds.
Main Results:
- Sulfhydryl amino acids (CysH, NAC) and DTT prolonged clotting time.
- CysH and NAC, when added before AcH, prolonged clotting more than AcH alone.
- HC and penicillamine reduced the AcH-induced prolongation of clotting time.
- Premixing serine, alanine, or lactalbumin hydrolysate with AcH diminished AcH's clotting prolongation effect.
Conclusions:
- Sulfhydryl-containing compounds and DTT influence clotting time.
- The interaction between AcH and certain amino acids, potentially forming cyclic adducts, affects clotting dynamics.
- Further research into adduct formation may clarify AcH's impact on coagulation.