Insulin A chain

Desiderio, D.M. Katakuse, I. FAB-MS of Insulin, Insulin A-Chain, Insulin B-Chain, and Glucagon. Biomed. Mass Spectrom. 1984,11, 55-59. 

Insulin A Chain 21 B Chain 20 21 Insertion 28 29 30 Functional Attributes"... 

FIGURE 13 Plot of the logarithm of the retention volume (In VR) versus the concentration of the displacing salt, ammonium sulphate, in the HP-HIC mode with the proteins I, insulin B-chain 2, bovine trypsin inhibitor 3, bovine trypsinogen 4, insulin A-chain 5, ribonuclease 6, sperm whale myoglobin 7, horse heart cytochrome c. Data from Ref. 42. 

Fig. 5. The separation of polypeptide standards on Hypersil ODS with 0.1 M NaHjP04-H3P04, pH 2.1, as the mobile phase, at a flow rate of 1 ml/min. The peaks are as follows 1, Trp 2, lysine vasopressin 3, arginine vasopressin 4, oxytocin, 5, ACTHj-j, 6, insulin A-chain 7, bombesin 8, substance P 9, somatostatin 10, insulin B-chain 11, human calcitonin 12, glucagon 13, salmon calcitonin 14, melittin. Adapted from Fig. I of O Hare and Nice (1979).

Cruz, N. Lopez, M. Estrada, G. Alvarado, X. de Anda, R. Baibas, R Gosset, G. Bolivar, F. Preparative isolation of recombinant human insulin-A chain by ion exchange chromatography. J.Liq.Chromatogr., 1992, 15, 2311-2324... 

Inbibin (activin), beta A Inhibin (activin), beta B Inbibin (activin), beta C Inhibin (activin), beta E Inhibin, alpha Insulin C-peptide Insulin, A chain Insulin, B chain Insulin-like growth factor lA Insulin-like growth factor II Inter-alpha trypsin inhibitor, HI Inter-alpha trypsin inhibitor, H2 Inter-alpha trypsin inhibitor, H4 Inter-alpha trypsin inhibitor, L Interferon alpha Interferon beta Interferon gamma Interleukin-1 beta Interleukin-10 Interleukin-12, alpha Interleukin-12, beta Interleukin-1 receptor antagonist Interleukin-2 Interleukin-4... 

The specificity of cathepsin L was studied with the insulin B-chain by Kargel et al. (52) and with a synthetic hexapeptide, luteinizing hormone-releasing hormone, neurotensin, and insulin A-chain by Katunuma et al. (48, 49). Their results are summarized in Fig. 3. Cathepsin L cleaves peptide bonds that have an apoleur amino acid such as Phe, Leu, Val, Trp, or Tyr in position Pj. The importance of hydrophobic amino acids in the P3 position has been suggested, but it is not so clear as for the Pj position. Apparently the amino acids in positions Pi and Pi make no contribution to the specificity. 

Fig. 3. Specificities of cathepsin L and cathepsin B toward hexapeptide, luteinizing hormone-releasing hormone, neurotensin, sind insulin A chain. The unbroken arrows indicate the m or sites of action of the enz3rmes, and the broken arrows indicate the minor sites of action. (From Ref. 45.)...

Figure 28.6 The primary sequence of the insulin A chain, a short polypeptide of 21 amino acids.

McLucket S. A. Herron, W. J. Stephenson, J. L., Jpl Goeringer, D. E. Cation attachment to multiply charged anions of oxidized bovine insulin A-chain. 

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