Presence in the Human Placenta and Term Serum of a Highly Lactogenic Substance Immunologically Related to Pituitary Growth Hormone

Josimovich, John B.; Maclaren, J. A.

doi:10.1210/endo-71-2-209

Cited by 351 publications

(70 citation statements)

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“…Later work by Josimovich and others revealed the presence of a protein hormone having lactogenic properties similar to human somatotropin [2 -51. Also termed human chorionic somatomammotropin [6], human placental lactogen [2] or human choriomammotropin, this hormone is now known to be a protein (see Fig. 4) of molecular weight 22500 having 191 residues and two disulfide bonds [7,8].…”

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confidence: 99%

Reaction of Human Choriomammotropin with Hydrogen Peroxide

Houghten

1977

European Journal of Biochemistry

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Treatment of human choriomammotropin with hydrogen peroxide in the absence of denaturant was found to oxidize five of its six methionine residues to sulfoxide; the residue not oxidized was found to be methionine‐170. This derivative was identical to the native hormone by exclusion chromatography, circular dichroism spectra, and rate of tryptic digestion, but suffered a very substantial drop in biological activity. In the presence of 8 M urea all of the methionines could be oxidized with hydrogen peroxide or alkylated with iodoacetic acid. The physical properties of these completely methionine‐modified derivatives were significantly changed and biological activity had again been very substantially decreased. In control experiments, treatment of the native hormone with 8 M urea did not affect its physical, spectral or biological properties. Amino acid analysis of the derivatives was completely in accord with that expected.

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confidence: 99%

Reaction of Human Choriomammotropin with Hydrogen Peroxide

Houghten

1977

European Journal of Biochemistry

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“…Yanai & Nagasawa, 1971;Foryth, 1973;Talamantes, 1975). Purification of the hormone has not yet been successful with three exceptions (Josimovich & MacLaren, 1962;Shome & Friesen, 1971;Fellows et al, 1974, probably because of the labile nature of this hormone (Grumbach & Kaplan;1964). Linkie & Niswender (1973) observed luteotropic activity in crude extracts and in Sephadex eluates of 25,000-50,000 MW from rat placentae, but no luteotropic activity was associated with any visible electrophoretic bands.…”

Section: Synopsismentioning

confidence: 99%

Synthesis of Two Lactogenic Proteins by the Mouse Placenta <I>in vitro</I>

Kohmoto

1975

Endocrinol Japon

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“…Placental lactogen hormones probably appeared about 75 million years ago (Martal, 1980) from a duplication of the growth hormone cistron. Though most of the members of this hormone family have specific biological properties, some of them such as hGH (Li, 1972), ovine PL Djiane, 1975, 1977 ;Martal, 1978), bovine PL (Murthy et al, 1982) or primate PL (Josimovitch and Mac Laren, 1962;Friesen, 1965;Kaplan and Grumbach, 1965 ;Florini et al, 1966 ;Shome and Friesen, 1971 ) Primate GH is the only animal GH efficient in humans. However, the memory of its common ancestral origin with the GH of other species is found both in the high percentage of identical primary structures (table 1 ) and in the fact that certain fragments of non-human GH exert a more or less pronounced biological effect in humans (Liberti and Miller, 1978 ;Maciag et al, 1980 ;Hubbard and Liberti, 1980).…”

Section: Introductionmentioning

confidence: 99%