Movement analysis in the early detection of newborns at risk for developing spasticity due to infantile cerebral palsy.

In order to limit the consequences of infantile cerebral palsy (ICP), physiotherapy should start as early as possible. This requires that infants at risk are detected at the earliest age possible. Today, diagnosis is based on visual observation by physicians and as such is influenced by subjective impressions. Objective methods, quantifying the pathological deviation from normal spontaneous motor activity would be preferable as they, for example, allow an inter- and intra-individual comparison of movement. In this paper we have developed a methodology that allows the 3-dimensional acquisition of unconstrained movement in newborn babies, using a motion analysis system. From the recorded movement data we have extracted 53 quantitative parameters that describe the differences between healthy and affected participants. Considered individually, each of these parameters does not permit a conclusive statement to be made as to whether or not the patient is at risk. Cluster analysis based on Euclidian distances therefore has been used to find an optimal combination of eight parameters. The optimal combination has been subsequently applied to organize the participants' movement into preferably homogeneous classes labelled "healthy" or "at risk". Classification was performed utilising quadratic discriminant analysis. The methodology presented allows a reliable discrimination between healthy and affected participants. Overall detection rate reached 73%. This value is expected to rise with increasing patient and norm collective database size.

The protein formula of beef heart cytochrome c oxidase.

Beef heart cytochrome c oxidase consist of 12 different polypeptides stoichiometrically arranged in respiratory complex IV. The functional 2 heme a, 2 copper monomer of this complex consist of 1793 amino acids; the exact Mr is 202,787 Da. From 17 cysteine residues, six are involved in the formation of three disulphide bonds. The theoretical heme a content of the enzyme is 9.86 nmol/mg protein. The theoretical iron and copper contents are 0.55 and 0.63 microgram/mg protein, respectively.

Studies on cytochrome-c oxidase, XIII. Amino-acid sequence of the small membrane polypeptide VIIIc from bovine heart respiratory complex IV.

The isolation and complete amino-acid sequence analysis of the cytoplasmically synthesized polypeptide VIIIc from bovine heart cytochrome-c oxidase is described. The protein is a stoichiometric constituent of the mitochondrial respiratory complex IV. Its primary structure is deduced from N-terminal sequencing and peptides obtained by enzymatic cleavage with Staphylococcus aureus proteinase and chemical cleavage with cyanogen bromide. The small protein consists of 56 amino acids summing up to a total Mr of 6243. From position 34 to 51 the chain contains a hydrophobic sequence of 18 residues. This probably membrane-spanning segment also contains the 2 cysteine residues of the chain. The function of this subunit in the respiratory complex IV is still unknown.

Studies on cytochrome c oxidase, XII. Isolation and primary structure of polypeptide VIb from bovine heart.

The isolation and complete sequence analysis of the cytoplasmically synthesized polypeptide VIb from bovine heart cytochrome c oxidase is described. The protein is a stoichiometric constituent of the respiratory complex IV. Its primary structure is deduced from N-terminal sequencing and overlapping peptides obtained from tryptic cleavage and specific cleavage at arginyl and tryptophyl peptide bonds. The polypeptide chain consists of 84 amino acids from which a Mr of 9419 is derived. It has a relatively high content of histidine and proline and contains a single cysteine. A hydrophobic sequence of 20 amino acids points to a membrane-penetrating structure similar to that found in polypeptides I, II, III, IV and VIIIa, VIIIb, VIIIc of the bovine oxidase. The sequence of VIb is tissue-specific, it contributes to the formation of nuclear coded isoenzymes of cytochrome c oxidase. The protein thus may be involved in a tissue-specific regulation of cellular respiration.

Studies on cytochrome c oxidase, X. Isolation and amino-acid sequence of polypeptide VIIIb.

The isolation and sequence determination of the cytoplasmically synthesized polypeptide VIIIb from beef heart cytochrome c oxidase is described. Several methods for isolating polypeptide VIIIb with gelchromatographic technics are presented. The complete amino-acid sequence is deduced from a N-terminal sequencer run, overlapping tryptic peptides and peptides obtained after tryptophan specific cleavage with cyanogen bromide in heptafluorobutyric acid/formic acid. The small protein consists of 46 amino acids and has a molecular mass of 4 962 Da. The existence of a hydrophobic segment with a length of 20 residues characterizes it as a membrane penetrating protein. The stoichiometry of this polypeptide in the functional monomer of cytochrome c oxidase (complex IV) is 2 and is thus different from all the other polypeptides constituting the respiratory complex IV. The function of this component of the terminal oxidase is as yet unknown.