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Biomedical subjects

H Lilie

Publications and source records attributed to H Lilie.

5 recordsLinked to original sources
PubMed1992

[The refusal to consent to blood transfusion. Legal and medical aspects using Jehovah's Witnesses as an example].

The limited understanding of a patient, such as a Jehovah's Witness, who has consented to an operation but refuses a blood transfusion for personal or religious reasons, places the physician in a moral dilemma. According to Article 2 II of the German Constitution, the fact that the patient has withheld or expressly refused his consent, i.e., in writing, mandates that the legal right of physical integrity be upheld with final legal effect, even in the case of an emergency. If this right to self-determination is abused, the person giving treatment is guilty of bodily harm in the sense of section 223 of the German Penal Code. Intraoperative haemodilution, the cell-save procedure, and colloidal and crystalloid volume replacement represent alternative methods of blood transfusion for Jehovah's Witnesses.

Blood Transfusion↗
PubMed1991

Alternatively folded states of an immunoglobulin.

Well-defined, non-native protein structures of low stability have been increasingly observed as intermediates in protein folding or as equilibrium structures populated under specific solvent conditions. These intermediate structures, frequently referred to as molten globule states, are characterized by the presence of secondary structure, a lack of significant tertiary contacts, increased hydrophobicity and partial specific volume as compared to native structures, and low cooperativity in thermal unfolding. The present study demonstrates that under acidic conditions (pH less than 3) the antibody MAK33 can assume a folded stable conformation. This A-state is characterized by a high degree of secondary structure, increased hydrophobicity, a native-like maximum wavelength of fluorescence emission, and a tendency toward slow aggregation. A prominent feature of this low-pH conformation is the stability against denaturant and thermal unfolding that is manifested in highly cooperative reversible phase transitions indicative of the existence of well-defined tertiary contacts. These thermodynamic results are corroborated by the kinetics of folding from the completely unfolded chain to the alternatively folded state at pH 2. The given data suggest that MAK33 at pH 2 adopts a cooperative structure that differs from the native immunoglobulin fold at pH 7. This alternatively folded state exhibits certain characteristics of the molten globule but differs distinctly from it by its extraordinary structural stability that is characteristic for native protein structures.

Amino Acids↗