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At least 91 records · Page 5Linked to original sources
PubMed1999

The kinematics of eating with a spoon: bringing the food to the mouth, or the mouth to the food?

In traditional reach-to-point and reach-to-grasp studies an increase in accuracy demands typically results in a lengthening of the deceleration phase of the reach and a freezing of the more distal joints. The purpose of the present experiment was to examine whether similar changes in the reach kinematics could be observed during a tool-using skill, as would be predicted from an effector independence perspective. Five subjects were required to eat two substances (i.e. a solid and a liquid one) that imposed different requirements on the accuracy of the movement. The subjects transported the substances from the plate into the mouth. A prolonged movement duration was found for the liquid as compared to the solid substance. However, rather than being exclusively due to a lengthening of deceleration phase, the larger movement duration resulted from a slowing down of the whole movement. Therefore, the skewed velocity profiles found in the traditional reach-to-grasp studies may well be the result of the accuracy demands only impinging on the final part of the movement trajectory, rather than being a consequence of central, effector-independent, organising principles. In addition, under increased accuracy demands subjects were shown to redistribute their movement in a proximodistal direction. Movements of the distal components were reduced to a minimum and the involvement of trunk and head movement increased.

Adult↗
PubMed1991

[Antigenic structure of the foot-and-mouth virus. VI. Functional segments of the immunodominant region of the VP1 protein of foot-and-mouth virus strains O1K and A22].

B- and T-epitopes have been localized within the protective fragments of VP1 protein, viz., 136-152 of the O1K strain and 135-159 of the A22 strain of the foot-and-mouth disease virus (FMDV). Antibodies eliciting after immunization of various animals with the 135-159 A22 peptide are directed to different sites of the peptide. Immunogenicity of fragments of the 135-159 A22 peptide on mice correlates with their activity on T-cells of the same animals and protective activity on guinea pigs. The investigations were carried out using synthetic fragments of the 136-152-O1K and 135-159-A22 peptides.

Amino Acid Sequence↗
PubMed1989

[Antigenic structure of the foot-and-mouth disease virus. III. Immunogenic properties of synthetic peptides of the sequence of the immunodominant region of VP1 proteins of the O1K and A22 strains of foot-and-mouth virus].

Immunogenic and protective properties of uncoupled and KLH-conjugated peptides covering the sequence of the immunodominant region of VP1 proteins of the O1K and A22 strains of foot-and-mouth disease virus have been studied. The uncoupled peptides 136-148 O1K, 136-152 O1K, 131-149 A22 and 140-149 A22 were shown to be immunogenic in guinea pigs and induced 50-100% protection against homologous virus. On the other hand, the A22 specific peptides, in contrast to the O1K peptides, were not immunogenic in rabbits. Immunization of nonresponders with the A22 specific peptides containing the O1K peptide can bypass nonresponsiveness to the A22 peptide in terms of the antibody production. The induced antibodies showed virus-neutralizing activity in vitro.

Amino Acid Sequence↗
PubMed1989

[Antigenic structure of foot-and-mouth virus. IV. Synthesis and immunogenic properties of new fragments of the VP1 protein of food-and-mouth virus strain A22].

A synthesis of new fragments of VP1 protein with the specificity of A22 strain of foot-and-mouth disease virus is described. Immunization with the free 136-152 peptide and KLH-conjugates of the peptides 136-152 and 197-213 induced 60-80% protection of guinea pigs against challenge with the A22 virus. Synthetic peptides corresponding to the 10-24, 50-69 and 175-189 sequences of VP1 did not show any protective activity. We have found that uncoupled peptides 175-189 and 197-213 are able to induce antipeptide antibodies. However, these antibodies did not possess any neutralizing activity. Immunization of animals with the mixture of (136-152)O1K and (175-189)A22 has led to inhibition of the immune response to the (136-152)O1K fragment.

Amino Acid Sequence↗