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1 SOBRE DICOM Y PACS

1.4 WADO: UNA OPCION PARA EL ACCESO VIA WEB

Gln-Glu Leu-Leu Asp-Cys Asp-Arg- - - - -Arg-Ser-Tyr

Gly-Gly-Tyr Pro-Trp-Ser-Ala-Leu Gln

Gln-Gln Val-Asp Asp-cys Ala-Lys-

Gly-Cys Lys

80 90

1 00

Phe-

Cys Asp-Val-

-

!le

Cys Arg-Ser-

1 1 0§

Ala-Leu-Gln-Asp-Gln-Lys-Tyr-Val-Thr-Ile Asp Thr-Tyr-Glu-Asn-Val-Pro-Tyr-Asn

Ar&-Glu-Lys-Gly-Pro-Tyr-Ala-Ala-Lys-Thr Asp Gly-Val-Arg-Gln-Val-Gln-Pro-Tyr Asn Gln-Gly-Ala-Leu-Leu­

Lys-Ala-Arg-Val-Pro-Arg Asn Asn-Glu-S.er-Ser-Met-

A p B F A p B F A p B F A p B F 130 1 40 1 50 - �hr-Ala-Val-Thr-Tyr ln-Pro

Tyr-Ser-Ile-Ala-Aan Gln-Pro Val-Ser-Val-Vel-Leu-Gln-Ala-Ala -Gly-Lys-Asp-Phe -Gln-Leu Tyr Arg-Gly Gly­ Tyr-Ala-Val-Ser-Lys Gln-Pro Ile-His-Ala-Val-Thr-Ala-Ile -Gly-Tyr

1 60 1 7 0

-Ala -Val Asp-His -Ale Ile-Val -Ile V� l-Gly-Tyr Gly-Thr-Glu-Gly-Gly-Vel-

Val Gly-Pro-cys-Gly Asp-His-Ala Val -Ala -Ala v� l-Gly-Tyr Asn- - - -Pro-

1 80

1 90

Lys-Aan-Ser-Trp Asp Thr Thr ly-Tyr Met Arg Ile -Leu

Gly Tyr Gly Thr Gly Trp-Gly-Glu Asn Gly-Tyr Ile Arg Ile-Lys

Arg Trp-Gly-Glu Ala Gly-Tyr Ile Arg

Gly-Gly-Ala- -

Gly-Asn-Ser-Tyr Val S er-S er-Ser-S er Ile

2 1 0 220

ys-Gly Leu -Tyr-Thr-s�-Ser-Phe Tyr-Pro Val -Lys-Asn-COOH ys-Gly Ile-Ala-Ile-Asp-Pro-Leu Tyr-Pro Thr-Glu-Gly

Fig. 4 . 4. Homologies among the available sequence s of some plant

tbiol prot eolytic enzymes.

2 00

Asn-V� l-

Gly -Thr-

Asp-Val-

Spaces in the sequenc es ind icate possible delet ions or insert ions of amino ac ids in the respec t ive protein sequences .

S equence numbering as for t he s equenc e of act inidin.

4 \H \N

The det ermination of t he primary amino acid s equenc e of ac t i nidin fro• the trypt ic pept ide s has provided the first c omplete amino ac id primary sequenc e of a plant t hiol prot ease t or c oaparison with the sequenc e o f papain. The d egre e ot ho� ol ogy among t he sequenc e s ot papain and actinidin , and the fragment s of s equenc e available for other plant thiol proteases, d emonstrates t hat the s tructural c haract eristics of ac t inidin are v ery similar to those d et ermined so far for other plant t hiol prot eases , thus providing further evidence for these enzymes having evolved from a commo n ancestral prot ein.

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