Steroid-protein interactions. III. Spectrophotometric demonstration of interaction between proteins and progesterone, deoxycorticosterone and cortisol

Westphal, Ulrich

doi:10.1016/0003-9861(57)90537-4

Cited by 48 publications

(14 citation statements)

References 16 publications

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“…The ability of albumin to bind a great number of steroids including cortisol has been abundantly established (2,(6)(7)(8). The factors determining the affinity with which albumin binds steroids differ from those which were observed with human plasma in the present experiments.…”

Section: Discussionmentioning

confidence: 99%

Binding of Corticosteroids by Plasma Proteins. Iii. The Binding of Corticosteroid and Related Hormones by Human Plasma and Plasma Protein Fractions as Measured by Equilibrium Dialysis12

Daughaday¹

1958

J. Clin. Invest.

168

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Section: Discussionmentioning

confidence: 99%

Binding of Corticosteroids by Plasma Proteins. Iii. The Binding of Corticosteroid and Related Hormones by Human Plasma and Plasma Protein Fractions as Measured by Equilibrium Dialysis12

Daughaday¹

1958

J. Clin. Invest.

168

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“…After 1 h at 2O"C, dithiothreitol and EDTA were removed by passage through Sephadex G-25 (Pharmacia-LKB, Milton Keynes, UK) equilibrated in buffer A. Albumin concentration was determined from the UV spectrum (~r,s = 3.89 x lo4 M-' . cm-' [17]). S-Nitrosylation of the albumin thiol was then achieved by incubation with a 5-fold molar excess of n-butyl nitrite at 37'C until no further increase in AsM was seen (approx.…”

Section: Rsno Preparationmentioning

confidence: 98%

Kinetics and equilibria of S‐nitrosothiol—thiol exchange between glutathione, cysteine, penicillamines and serum albumin

Meyer¹,

Kramer²,

Özer³

et al. 1994

FEBS Letters

153

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AbShCtThe kinetics and equilibria of S-nitrosothiol-thiol (SNO-SH) exchange reactions were determined using differential optical absorption. At pH 7.4and 37'C, k2 values ranged from 0.9 M-i . s-' for the reaction between S-nitroso-glutathione (GSNO) and N-acetyl-penicillamine, and up to 279 M-' . se1 for the exchange between S-nitroso-penicillamine (penSNO) and GSH. SNO-SH exchange involving GSIWGSNO and cysteine/cySNO was relatively rapid, k, approx. 80 M-' . s-' with an equilibrium constant slightly in favour of GSNO. GSNO was strongly favoured in equilibrium with penSNO, k, 0.0039. In the case of SNG-SH exchange between S-nitroso human serum albumin (albSN0) and GSH or cysteine k2 values were 3.2 and 9.1 M-i . s-l, respectively. The results show that the initial rate of SNO-SH exchange between physiological albSN0 (7 @I) and venous plasma levels of GSH and cysteine is very slow, < l%/min. On the other hand, if a nitrosothiol such as cySN0 were to enter a cell, it would be rapidly converted to GSNO (43%/s).

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“…Steroid-binding proteins are glycoproteins that transport hormones of the hypothalamic–pituitary–adrenal (HPA) and hypothalamic–pituitary–gonadal (HPG) axes to target tissues (Westphal, 1983; Breuner and Orchinik, 2002). The function of binding globulins is much debated.…”

Section: Neuroendocrine Advances: Improving Understanding Of Social Vmentioning

confidence: 99%

Towards an integrative understanding of social behavior: new models and new opportunities

Blumstein¹

2010

Front. Behav. Neurosci.

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Social interactions among conspecifics are a fundamental and adaptively significant component of the biology of numerous species. Such interactions give rise to group living as well as many of the complex forms of cooperation and conflict that occur within animal groups. Although previous conceptual models have focused on the ecological causes and fitness consequences of variation in social interactions, recent developments in endocrinology, neuroscience, and molecular genetics offer exciting opportunities to develop more integrated research programs that will facilitate new insights into the physiological causes and consequences of social variation. Here, we propose an integrative framework of social behavior that emphasizes relationships between ultimate-level function and proximate-level mechanism, thereby providing a foundation for exploring the full diversity of factors that underlie variation in social interactions, and ultimately sociality. In addition to identifying new model systems for the study of human psychopathologies, this framework provides a mechanistic basis for predicting how social behavior will change in response to environmental variation. We argue that the study of non-model organisms is essential for implementing this integrative model of social behavior because such species can be studied simultaneously in the lab and field, thereby allowing integration of rigorously controlled experimental manipulations with detailed observations of the ecological contexts in which interactions among conspecifics occur.

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Steroid-protein interactions. III. Spectrophotometric demonstration of interaction between proteins and progesterone, deoxycorticosterone and cortisol

Cited by 48 publications

References 16 publications

Binding of Corticosteroids by Plasma Proteins. Iii. The Binding of Corticosteroid and Related Hormones by Human Plasma and Plasma Protein Fractions as Measured by Equilibrium Dialysis12

Binding of Corticosteroids by Plasma Proteins. Iii. The Binding of Corticosteroid and Related Hormones by Human Plasma and Plasma Protein Fractions as Measured by Equilibrium Dialysis12

Kinetics and equilibria of S‐nitrosothiol—thiol exchange between glutathione, cysteine, penicillamines and serum albumin

Towards an integrative understanding of social behavior: new models and new opportunities

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