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Biomedical subjects

M Pras

Publications and source records attributed to M Pras.

At least 163 records · Page 9Linked to original sources
PubMed1977

Protracted arthritis in familial Mediterranean fever.

A review of the files of familial Mediterranean fever (FMF) confirmed the rarity of patients suffering protracted arthritic attacks and the propensity of the joints, in general, to recover. While 70% of those afflicted suffered bouts of synovitis, only 57 patients (5% of the FMF-population) experienced protracted attacks involving a total of 84 joints, 36 of them knees and 25 hips. Functional and, usually, anatomical integrity was regained in all but 27 joints. Of the 27 joints producing residual incapacity, 21 were hips. Seven hips showed roentgenologically typical aseptic necrosis of the femoral head and 14 only sclerosis and narrowing of the joint space. Eight hips eventually required total prosthetic replacement. We suggest that the poor prognosis of the hip, in contrast to other joints affected by protracted FMF-arthritis, is related not directly to the metabolic aberrration underlying the disease but to attenuation of the arterial blood supply of the femoral head by synovial exudation. Early aspiration of exudate could alter the prognosis by preventing the complication of aseptic necrosis.

Adolescent↗
PubMed1977

The amino acid sequence of duck amyloid A (AA) protein.

AA protein constitutes 50 to 60% of the amyloid fibrils from livers of ducks developing spontaneous amyloidosis and has a m.w. of about 12,000. The sequence of the first 73 residues was established by automatic Edman degradation of the whole molecule and isolated cyanogen bromide fragments, and corroborated by placement of tryptic peptides. The sequence from position 76-80 was tentatively derived from a peptide that was homologous to that region of human and monkey AA proteins. Carboxypeptidase digestion showed the carboxy terminal sequence to be Ala, Arg, with some heterogeneity (Ser, Arg). Compared to human AA protein, there were five additional residues at the amino terminus. In view of the m.w. and the existence of additional peptides an extension at the C-terminal end seems likely. Sequence homologies to other AA proteins are discussed.

Amino Acid Sequence↗
PubMed1973

Immunologic studies of the major nonimmunoglobulin protein of amyloid. I. Identification and partial characterization of a related serum component.

Antisera have been prepared against the major nonimmunoglobulin component of secondary and familial Mediterranean fever (FMF) associated amyloid which has been called A component or acid soluble fraction (ASF). The antisera were shown to be monospecific for ASF by precipitation of (125)I-labeled antigen and gave a reaction of identity with four different ASF preparations. The antisera were able to detect a circulating component in human serum that migrated in the alpha1-globulin region. This circulating component gave a line of identity with degraded ASF by double immunodiffusion. 57 normal sera and 89 sera from patients with diseases known to be frequently associated with amyloidosis were tested by immunodiffusion for the circulating ASF component. 7% of normal sera and 50-80% of the pathologic sera had elevated amounts of this component. Absorption studies showed that all normal sera probably have small amounts of this component while cord sera do not have detectable amounts. This component was partially purified and was shown to be slightly larger than albumin. The relation of the circulating component to the acid soluble fraction of amyloid is discussed.

Absorption↗