Hormone sequences, table

The amino acid sequence of insulins from various animal species has been examined. Details of these are shown in Table 25-6. Il is apparent from the antilysis that frequent changes in sequence occur within the inlerehain di.sulfide ring (positions 8, 9, and 10). The hormonal. sequence fur porcine insulin is the closest lo lhal of humans, differing... 

At the time of the discovery of Met-enkephalin, its sequence was observed to be identical to that of residues 61—65 contained in the C-fragment of the pituitary hormone p-Hpotropin [12584-99-5] (p-LPH) (see Hormones), first isolated in 1964 (11). In 1976, the isolation of a larger peptide fragment, P-endorphin [60617-12-1] that also displayed opiate-like activity was reported (12). This peptide s 31-amino-acid sequence comprised residues 61—91 of P-LPH. Subsequentiy, another potent opioid peptide, dynorphin [72957-38-17, was isolated from pituitary (13). The first five amino acids (qv) of this 17-amino-acid peptide are identical to the Leu-enkephalin sequence (see Table 1). 

Table 43-1. The DNA sequences of several hormone response elements (HREs). ...

In the ebb phase, there is increased activity of the sympathetic nervous system and increased plasma levels of adrenaline and glucocorticoids but a decreased level of insulin. This results in mobilisation of glycogen in the liver and triacylglycerol in adipose tissue, so that the levels of two major fuels in the blood, glucose and long-chain fatty acids, are increased. This is, effectively, the stress response to trauma. These changes continue and are extended into the flow phase as the immune cells are activated and secrete the proinflammatory cytokines that further stimulate the mobilisation of fuel stores (Table 18.2). Thus the sequence is trauma increased endocrine hormone levels increased immune response increased levels of cytokines metabolic responses. 

HORMONES OF THERAPEUTIC INTEREST 345 Table 8.13. GnRH and some of its analogues, along with their amino acid sequence... 

The steroid hormone receptors are sequence specific DNA binding proteins whose cognate DNA elements are termed hormone responsive elements" (HREs). The HREs known to date possess a common structure. They are composed primarily of two copies of a hexamer sequence. In table 4.1 are listed the hexamer sequences of the HREs of important nuclear receptors. 

The final peptide structure shown in Table 2 represents an insect sulfakinin recently isolated from br-cc/ca extracts of the locust, Locusta migratoria. and structurally characterized. A modification of the four-step HPLC purification system (10) in which all gradients were extended to a higher final acetonitrile concentration was utilized. In addition, a C-8 reverse-phase column was substituted for the C-18 column (Schoofs, L., et al. Chromatography and Isolation of Insect Hormones and Pheromones, in press.). The isolated hindgut of L. maderae was used as the bioassay. Lom-SK contains residues of Leu and Ala at the 2- and 3-positions, respectively. The remainder of the sequence is identical with the 2-10 sequence of LSK-II. 

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