{"_buckets": {"deposit": "f7134ecd-6409-4005-b124-3592ecb74095"}, "_deposit": {"id": "4905", "owners": [], "pid": {"revision_id": 0, "type": "depid", "value": "4905"}, "status": "published"}, "_oai": {"id": "oai:nagoya.repo.nii.ac.jp:00004905", "sets": ["645"]}, "author_link": ["12223", "12224"], "item_12_biblio_info_6": {"attribute_name": "書誌情報", "attribute_value_mlt": [{"bibliographicIssueDates": {"bibliographicIssueDate": "1997-10-31", "bibliographicIssueDateType": "Issued"}}]}, "item_12_date_granted_64": {"attribute_name": "学位授与年月日", "attribute_value_mlt": [{"subitem_dategranted": "1997-10-31"}]}, "item_12_degree_grantor_62": {"attribute_name": "学位授与機関", "attribute_value_mlt": [{"subitem_degreegrantor": [{"subitem_degreegrantor_language": "ja", "subitem_degreegrantor_name": "名古屋大学"}, {"subitem_degreegrantor_language": "en", "subitem_degreegrantor_name": "NAGOYA University"}], "subitem_degreegrantor_identifier": [{"subitem_degreegrantor_identifier_name": "13901", "subitem_degreegrantor_identifier_scheme": "kakenhi"}]}]}, "item_12_degree_name_61": {"attribute_name": "学位名", "attribute_value_mlt": [{"subitem_degreename": "博士(農学)", "subitem_degreename_language": "ja"}]}, "item_12_description_4": {"attribute_name": "抄録", "attribute_value_mlt": [{"subitem_description": "Peptidal growth factors were isolated from conditioned medium derived from rice (Oriza sativa L.) suspension cultures and identified to be a sulfated pentapeptide(Htyr (SO3H)-Ile-Tyr (SO3H)-Thr-Gln-OH）and its C-terminal truncated tetrapeptide (Htyr (SO3H)-Ile-Tyr(SO3H)-Thr-OH).These structures were identical to the phytosulfokines originally found in asparagus (Asparagus officinalis L.) mesophyll cultures. The pentapeptide phytosulfokine-α(PSK-α) very storongly stimulated colony formation of rice protoplasts at concentrations above 10-8 M, indicating a species-independent mode of action of phytosulfokines. Binding assays using 35S-labeled phytosulfoking sites on the surface of rice cells in susupension. Analysis of [35S]PSK-α binding in differential centrifugation fractions suggested association of the binding with a plasma membrane -enriched fraction. The apparent Kd values for[35S]PSK-αbinding was found to be 1 x 10-9 M for the high affinity type and 1 x 10-7 M for the low affinty type, with maximum numbers of binding sites of 1 x 104 sites/cell and 1 x 105 sites/cell, respectively. Competition studies with the [35S]PSK-αand several synthetic PSK-αanalogs demonstrated that only peptides which possesses mitogenic activity can effectively displace the radioligand. 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