Biochemical analysis of teleost melanin-concentrating hormone

dc.creatorBird, Dinah Frances
dc.date.accessioned2016-11-14T23:11:25Z
dc.date.available2011-02-19T01:09:09Z
dc.date.available2016-11-14T23:11:25Z
dc.date.issued1979-08
dc.degree.departmentZoologyen_US
dc.description.abstractA series of experiments was conducted to examine the gross biochemical nature of melanin-concentrating hormone (MCH) by utilizing a reliable and simple ^H vivo bioassay. Boiling and trypsin digestion of cod pituitary homogenate supernantant containing MCH destroyed the MCH activity. Dialysis indicated MCH was between 3,500 and 13,000 rr.olecular weight. MCH is a cation; as it bound to CM cellulose but did not bind to DEAE cellulose. Disulfide bonds apparently were not present in MCH since sodium borohydride did not disrupt MCH activity. In the Killifish, MCH activity was not found in the brain. Evidence presented here suggests -MCH is a small positively charged polypeptide containing no disulfide bonds.
dc.format.mimetypeapplication/pdf
dc.identifier.urihttp://hdl.handle.net/2346/22683en_US
dc.language.isoeng
dc.publisherTexas Tech Universityen_US
dc.rights.availabilityUnrestricted.
dc.subjectBiological assayen_US
dc.subjectMelaninsen_US
dc.subjectTeleosteien_US
dc.subjectPituitary hormonesen_US
dc.titleBiochemical analysis of teleost melanin-concentrating hormone
dc.typeThesis

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