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PMID:2776635
| Citation |
Schoon, DV, Enomoto, H and Harris, MP (1989) Age-related changes in the first order Weiner kernel visual evoked potential. Doc Ophthalmol 71:329-40 |
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| Abstract |
Visual evoked potentials were obtained from 112 subjects (215 eyes) aged 5 to 79 years with fast random stimuli. The stimulus (the presence or absence of the initiation of a reversal) and response (voltage measurements) were used in calculating the first order Wiener kernels to obtain the visual evoked potentials. Five check sizes were used to stimulate each eye. The implicit time of the major negative wave showed a significant increase with age for each check size used. Regression lines for the implicit time vs age data for male subjects were significantly different from those of females. The y-intercepts were lower and the slope of the regression lines were consistently steeper for males. Thus the rate of increase in implicit time was higher in males. The relationship of the amplitude of the major wave to age did not appear to be linear. The data suggested that a second-order polynomial curve might be an appropriate representation of the relationship. |
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| Keywords |
Adolescent; Adult; Aged; Aging/physiology; Child; Child, Preschool; Evoked Potentials, Visual; Female; Humans; Male; Middle Aged; Sex Factors; Vision, Ocular/physiology; Visual Acuity |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004175: endopeptidase activity |
ECO:0000247: |
UniProtKB:K7NPX3
|
F |
The predicted endolysin (ADE34958) of phage KP15 is very similar to the endolysin (AEX26632) of phage KP27. The only difference is only in one amino acid (glutamic acid of KP15 endolysin is replaced by glutamine in the KP27 endolysin in the seventeenth position from N-terminus) (results section, subsection; Description of KP15 and KP27 lysis system). Figure 4 AND S4 show the digestion of E. coli peptidoglycan sacculus KP27 endolysin and shows that KP27 endolysin is a l-alanyl-d-glutamate endopeptidase. It further shows that KP27 endolysins has an endopeptidase activity cleaving between l-Ala and d-Glu of the stem peptide and no d-alanyl-d-alanine carboxypeptidase activity. |
complete | |||
Notes
See also
References
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