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Biomedical subjects

M Zajdel

Publications and source records attributed to M Zajdel.

12 recordsLinked to original sources
PubMed1994

Interactive method of informing patients of the risks of intravenous contrast media.

PURPOSE: To evaluate interactive computer-based informed consent for use of contrast material versus the same information in a written format. MATERIALS AND METHODS: Patients (n = 160) referred for radiologic examination with intravenous contrast material were block randomized (sex, age, and previous exposure to contrast material) into two groups and were provided either written or computer-based (video) informed consent. RESULTS: The female patients in the video group scored better on the test than those in the group with the written consent form. Male patients attained equivalent scores with both types of consent. The video took an average of 1.6 minutes longer to complete, probably because the majority of patients chose to be informed of every risk of intravenous contrast material. CONCLUSION: This project demonstrates that a video format for informed consent before use of intravenous contrast material offers a good alternative to the written consent form.

Comprehension↗
PubMed1976

Studies on chemically modified fibrinogen.

Treatment of fibrinogen with maleic acid anhydride renders fibrinogen unclottable depending on the degree of modification of the molecule. According to radioactive studies the release of fibrinopeptides by thrombin or reptilase is undisturbed. The incoagulability is due to inhibition of the polymerization process of fibrinmonomers derived from modified fibronogen, mainly caused by the increase of electronegative charges upon the fibrogen molecule. According to discelectrophoretic analysis modified fibrinogen fails to produce fragments D and E following plasmic digestion, however, may be degraded to high molecular weight products. Modified fibrinogen reveals some similarities to abnormal fibrinogens in congenital dysfibrinogenemia with regard to its functional properties.

Anhydrides↗
PubMed1975

Amino-acid sequence of activation cleavage site in plasminogen: homology with "pro" part of prothrombin.

A 38-residue fragment is isolated from carboxymethylated plasminogen. Residues 29-38 have the same sequence as the amino-terminal end of the light chain of plasmin. The sequence 1-28 is therefore the sequence of the carboxyl-terminal end of the heavy chain and contains the specific sequence at which urokinase (EC 3.4.99.26) and other plasminogen-activating serine proteases split. Two of the five carboxymethyl-cysteine residues in the isolated fragment are situated close to the cleavage site and the fragment is not itself a substrate for plasminogen-activators. Residues 1-11 show extensive sequence homology with residues 137-147 and 242-252 in prothrombin, which are located in corresponding regions of the two internally homologous 83-residue structures in the non-thrombin part of the molecule, indicating that such structures may be a common feature of the non-protease part of the larger serine protease zymogens.

Amino Acid Sequence↗