| 产品描述： | Protoporphyrin-9 is the key porphyrin in animal and plant cells, presenting a precursor scaffold for heme sites and other metal domains contained in metalloproteins. Iron is introduced to the porphyrin to generate heme, the primary oxygen-binding moiety found in proteins. Protoporphyrin-9 as heme is incorporated into hemoglobin, catalase, peroxidase, and certain cytochrome enzymes. Introduction of magnesium into Protoporphyrin-9 and subsequent transformations generates chlorophyll, the main light energy-gathering pigment in plants necessary for photosynthesis. Protoporphyrin-9 is also demonstrated to activate guanylate cyclase, indicating that cellular levels of Protoporphyrin-9 and heme may serve to regulate guanylate cyclase activity and tissue cyclic GMP levels. λex 402 nm, 409 nm λem 625 nm, 633 nm;Protoporphyrin-9 is the key porphyrin in animal and plant cells, presenting a precursor scaffold for heme sites and other metal domains contained in metalloproteins. Iron is introduced to the porphyrin to generate heme, the primary oxygen-binding moiety found in proteins. Protoporphyrin-9 as heme is incorporated into hemoglobin, catalase, peroxidase, and certain cytochrome enzymes. Introduction of magnesium into Protoporphyrin-9 and subsequent transformations generates chlorophyll, the main light energy-gathering pigment in plants necessary for photosynthesis. Protoporphyrin-9 is also demonstrated to activate guanylate cyclase, indicating that cellular levels of Protoporphyrin-9 and heme may serve to regulate guanylate cyclase activity and tissue cyclic GMP levels. λex 402 nm, 409 nm λem 625 nm, 633 nmActivates soluble guanylyl cyclase. The precursor to heme sites and chlorophyll |
上海工商
危险品化学品经营许可证（不带存储）
营业执照(三证合一)
北京