The Effects of Two Different Rest Intervals on the Repeated Skating Ability of Ice Hockey Forwards and Defensemen.

The purpose of this study was to evaluate the effects of two different rest intervals (2 min and 3 min), between two consecutive sets of repeated sprint skating ability (RSSA) tests, on the repeated sprint ability of ice hockey Forwards and Defensemen. Two protocols of RSSA tests, RSSA-2 and RSSA-3, were completed by 16 ice hockey Forwards and 8 Defensemen. Defensemen were heavier (p < 0.

Effect of Rest Period Duration between Sets of Repeated Sprint Skating Ability Test on the Skating Ability of Ice Hockey Players.

The aim of this study was to determine the effects of two different rest periods, 2 min and 3 min, between consecutive sets of a repeated sprint skating ability (RSSA) test, on the skating ability of ice hockey players. Two RSSA tests, RSSA-2 and RSSA-3, were assessed on 24 ice hockey players. In RSSA-2, six sets of 3 × 80 m sprint skating, with 2 min passive recovery between two consecutive sets was allowed.

'Wave-type' structure of a synthetic hexaglycosylated decapeptide: a part of the extracellular domain of human glycophorin A.

The three-dimensional structure of a glycopeptide, His-Thr*-Ser*-Thr*-Ser*-Ser*-Ser*-Val-Thr-Lys, with 2-acetamido-2-deoxy-alpha-D-galactose (GalNAc) residues linked to six adjacent amino acids from Thr-10 to Ser-15, was studied by NMR spectroscopy and molecular dynamics (MD) simulations. The hexaglycosylated decapeptide is part of the extracellular domain of human glycophorin A and shows an extended structure of the peptide backbone due to O-glycosylation. Furthermore, each GalNAc residue exhibits one and only one NOE contact from the NHAc proton to the backbone amide proton of the amino acid that the sugar is directly bound to.

Synthesis of an N-glucoasparagine analog as a building block for a V3-loop glycopeptide from gp120 of HIV-I.

The preparative synthesis of a new N4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-L-asparagine mimetic 1, starting from 2-amino-1,5-anhydro-2-deoxy-glucitol hydrochloride and Z-Asp-(OH)-OBn is described. This glycosyl-amino acid unit 1 is expected to show higher stabilities towards in vivo conditions. Further, the use of 1 as building block for the synthesis of modified glycopeptides using solid phase support is reported.

Enhanced binding of antibodies to the DTR motif of MUC1 tandem repeat peptide is mediated by site-specific glycosylation.

The epithelial mucin MUC1 is an important tumor marker of breast cancer and other carcinomas. Its immunodominant DTR motif, which is the principal target for immunotherapeutic approaches, has been assumed until recently not to be glycosylated in both normal and tumor MUC1 and to acquire its immunogenic conformation by virtue of a certain number of tandem repeats. We present evidence that the antigenicity of the single repeat toward a considerable number of antibodies to the DTR motif is greatly enhanced if it is glycosylated within this motif, and only in this position.