[Relations of iodination, hormonosynthesis and proteolytic cleavage in human thyroglobulin].
Normally iodinated thyroglobulin (Tg) contains low molecular weight hormone-rich peptides associated to the bulk of the molecule by disulfide bridges. It is shown, with the assistance of in vitro iodination experiments using different iodine concentrations and various incubation times, that the proteolytic cleavage giving rise to the 26 K hormonopeptide in human Tg is part of a coupling reaction rather than iodination. This cleavage may be a preliminary event related to a facilitation in the release of thyroid hormones.
Lejeune
P J
PJ
Laboratoires de Chimie biologique et de Biochimie médicale associés au C.N.R.S., U.A. n. 178 et U. n. 38 de l'I.N.S.E.R.M., Faculté de Médecine, Marseille.
Marriq
C
C
Rolland
M
M
D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007455:Iodine / Q000378:metabolism*; D010084:Oxidation-Reduction; D013954:Thyroglobulin / Q000378:metabolism*
D013954:Thyroglobulin; D007455:Iodine
Relation entre iodation, hormonosynthèse et clivages protéolytiques dans la thyroglobuline humaine.