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L Miterová

Publications and source records attributed to L Miterová.

9 recordsLinked to original sources
PubMed1991

Use of the metal replica technique in the electron microscopy of collagen.

The authors present a survey of visualization of the individual types of collagen by the metal replica technique, special attention was paid to the visualization of type IX collagen, which, together with type XI, is a minor component of cartilage collagen. The molecule of this collagen type contains three collagen and four non-collagen domains and during the isolation involving pepsin digestion it is cleaved into MHW and LMW fragments. The HMW fragment can be further cleaved into shorter and longer arm. Results of statistical evaluation of 199 measured molecular fragments showed the following length: whole molecule 194 +/- 23 nm, HMW 136 +/- 16 nm, the longer arm of the HMW 87 +/- +/- 12 nm and the LMW of shorter arm of the HMW 43 +/- 9 nm.

Collagen↗
PubMed1989

Comparison of two methods for evaluation of the length of collagen molecules.

Two microscopical methods for the evaluation of molecular length--the measurement of SLS aggregates and the rotary shadowing technique--are compared. Two types of collagen were used for the comparison: type I collagen, isolated by acid extraction from calf skin, and type IX, isolated from chicken cartilage. An average length of 303 nm was obtained for type I collagen (by measurement of SLS aggregates 247 nm). Type IX collagen forms three different types of SLS crystallites corresponding to molecular lengths of 61, 95 and 206 nm; with the rotary shadowing technique, lengths of 84, 116 and 197 nm were measured.

Animals↗
PubMedDate not supplied

Contribution to the mode of action of univalent gold.

Au+ binds to the collagen structure and, therefore, the authors studied the kinetics of the interaction between sodium gold thiosulphate (SGTS) and C1q complement subcomponent, the structure of is partially collagenous. The kinetics was evaluated densitometrically and compared with that of collagen and SGTS. On the basis of those results, the effect of SGTS upon collagen type-II-induced arthritis (CIA) was investigated in Wistar rats. SGTS (20 mg per kg of body weight weekly) was administered i.m. starting i) with the first immunization dose, ii) with the second immunization dose, and iii) after the onset of arthritis. Regardless of the timing of drug administration the manifestation of arthritis was decreased, but the decrease was more expressed in the first two groups. It was concluded that SGTS administration is capable of inhibiting CIA, provided that the drug is applied sufficiently early. Since formation of antibodies to type-II collagen remained unaffected, it is feasible that the mode of action of gold complexes is based mainly on blocking the activation of complement system.

Animals↗