Gait analysis is a valuable tool for obtaining quantitative information on motor deficits in Parkinson's disease (PD). Since the characteristic gait patterns of PD patients may not be fully identified by brief examination in a clinic, long-term, and unobtrusive monitoring of their activities is essential, especially in a nonclinical setting. This paper describes a single accelerometer-based gait analysis system for the assessment of ambulatory gait properties. Acceleration data were recorded continuously for up to 24 h from normal and PD subjects, from which gait peaks were picked out and the relationship between gait cycle and vertical gait acceleration was evaluated. By fitting a model equation to the relationships, a quantitative index was obtained for characterizing the subjects' walking behavior. The averaged index for PD patients with gait disorder was statistically smaller than the value for normal subjects. The proposed method could be used to evaluate daily gait characteristics and thus contribute to a more refined diagnosis and treatment of the disease.

Gait analysis is widely recognized as a promising tool for obtaining objective information on the walking behavior of Parkinson's disease (PD) patients. It is especially useful in clinical practices if gait properties can be captured with minimal instrumentation that does not interfere with the subject's usual behavioral pattern under ambulatory conditions. In this study, we propose a new gait analysis system based on a trunk-mounted acceleration sensor and automatic gait detection algorithm. The algorithm identifies the acceleration signal with high intensity, periodicity, and biphasicity as a possible gait sequence, from which gait peaks due to stride events are extracted by utilizing the cross-correlation and anisotropy properties of the signal. A total of 11 healthy subjects and 12 PD patients were tested to evaluate the performance of the algorithm. The result indicates that gait peaks can be detected with an accuracy of more than 94%. The proposed method may serve as a practical component in the accelerometry-based assessment of daily gait characteristics.

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A new sweet protein, named mabinlin 11, was extracted with 0.5 M NaCl solution from the seeds of Capparis masaikai L i d . and purified by ammonium sulfate fractionation, carboxymethylcelluloseSepharose ion-exchange chromatography and gel filtration. The sweetness of mabinlin I1 was unchanged by at least 48 h incubation at nearly boiling temperature. Purified mabinlin I1 thus obtained gave a single band having a molecular mass of 14 kDa on SDS/PAGE. In the presence of dithiothreitol, mabinlin I1 gave two bands having molecular masses of 4.6 kDa and 5.2 kDa on SDS/PAGE. Two peptides (A chain and B chain) were separated from reduced and S-carboxamidomethylated mabinlin I1 by HPLC. The amino acid sequences of the A chain and B chain were determined by the automatic Edman-degradation method. The A chain and B chain consist of 33-amino-acid and 72-amino-acid residues, respectively. The A chain is mostly composed of hydrophilic amino acid residues and the B chain also contains many hydrophilic residues. High similarity was found between the amino acid sequences of mabinlin I1 and 2s seed storage proteins, especially 2s albumin AT2S3 in Arabidopsis thaliuna (mouse-ear cress).Plants of Capparis masaikai Levl. (local name mabinlang) grow in the subtropical region of the Yunnan province of China and bear fruits of tennis-ball size. The matured seed is used as a traditional Chinese medicine and elicits a sweet taste. Natives commonly chew the seeds for their sweetness. One of authors, Hu Zhong [l -41 and his coworkers, first isolated two sweet proteins from the seed and named them mabinlin I and 11. According to his report, mabinlin I1 is highly heat stable, which is different from other sweet proteins, thaumatin [5] and monellin [6]. In spite of this interesting property of mabinlin, an attempt to determine its primary structure has not been made, probably because the mabinlin sample isolated was not completely pure.In the present study, we have established a method for isolation of mabinlin from the seeds of C. masaikai and purified five homologues of mabinlin. Since mabinlin I1 was most heat stable among these homologues, we determined the complete amino acid sequence of mabinlin 11. Mabinlin I1 is composed of an A chain with 33-amino-acid residues which are mostly hydrophilic and the B chain with 72 residues. The origin of the heat stability of mabinlin I1 is discussed.

The oligosaccharide structures of Cry j I, a major allergenic glycoprotein of Cryptomeria japonica (Japanese cedar, sugi), were analysed by 400 MHz 1H-NMR and two-dimensional sugar mapping analyses. The four major fractions comprised a series of biantennary complex type N-linked oligosaccharides that share a fucose/xylose-containing core and glucosamine branches including a novel structure with a nongalactosylated fucosylglucosamine branch. Rabbit polyclonal anti-Cry j I IgG antibodies cross-reacted with three different plant glycoproteins having the same or shorter N-linked oligosaccharides as Cry j I. ELISA and ELISA inhibition studies with intact glycoproteins, glycopeptides and peptides indicated that both anti-Cry j I IgGs and anti-Sophora japonica bark lectin II (B-SJA-II) IgGs included oligosaccharide-specific antibodies with different specificities, and that the epitopic structures against anti-Cry j I IgGs include a branch containing alpha 1-6 linked fucose and a core containing fucose/xylose, while those against anti-B-SJA-II IgGs include nonreducing terminal mannose residues. The cross-reactivities of human allergic sera to miraculin and Clerodendron Trichotomum lectin (CTA) were low, and inhibition studies suggested that the oligosaccharides on Cry j I contribute little or only conformationally to the reactivity of specific IgE antibodies.