Amino Acid Composition of Cockroach Hypertrehalosaemic Hormones

1985 ◽  
Vol 40 (1-2) ◽  
pp. 42-46 ◽  
Author(s):  
Gerd Gäde

Hypertrehalosaemic hormones I and II from the corpus cardiacum of the American cockroach (Periplaneta americana) were separated by reversed-phase high-performance liquid chromato­graphy using a Nucleosil C18 column with a trifluoroacetic acid/acetonitrile gradient. The eluent was monitored at 206 nm and the hypertrehalosaemic activity detected by bioassay. The amino acid compositions of hypertrehalosaemic hormone I and II were determined after acid hydrolysis with HCl or methanesulfonic acid. Both neurohormones are octapeptides. Hypertrehalosaemic hormone I contained the amino acids Asp(2), Ser, Glu, Pro, Val, Phe and Trp, whereas hyper­trehalosaemic hormone II contained the amino acid residues Asp, Thr(2), Glu, Pro, Leu, Phe and Trp.

1990 ◽  
Vol 69 (11) ◽  
pp. 1717-1723 ◽  
Author(s):  
T. Xu ◽  
E. Telser ◽  
R.F. Troxler ◽  
F.G. Oppenheim

A major macaque histatin (M-histatin 1) from the parotid secretion of the subhuman primate, Macaca fascicularis, was isolated by gel filtration on Bio-Gel P-2 and purified to homogeneity by reversed-phase high-performance liquid chromatography on a TSK-ODS C18 column. The complete amino acid sequence of M-histatin 1, determined by automated Edman degradation, is: 1 10 20 Asp-Pse-His-Glu-Glu-Arg-His-His-Gly-Arg-His-Gly-His-His-Lys-Tyr-Gly-Arg-Lys-Phe 21 30 38 His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr-Arg-Ser-Asn-Tyr-Leu-Tyr-Asp-Asn M-histatin 1 contains 38 amino acid residues, a phosphoserine at residue 2, has a molecular weight of 4881.8, a calculated pI of 8.5, and histidine forms 26.3% of the mass. The hydropathicity plot of M-histatin 1 predicts that the molecule is entirely hydrophilic, and Chou-Fasman secondary prediction indicates that the polypeptide is devoid of alpha-helix and beta-sheet conformation in aqueous solutions but contains a series of beta turns. M-histatin 1 includes a six-amino-acid insert (residue 10-15) not present in human histatins and, with the introduction of gaps to maximize homology, it displays 89% and 91% sequence similarity with human histatins 1 and 3, respectively. M-histatin 1 exhibited fungicidal and fungistatic effects against the dimorphic pathogen, Candida albicans, in three separate bioassays. Its anticandidal effects were comparable with or greater than those of human histatins 1, 3, and 5. M-histatins 2, 3, and 4 were not sequenced directly because insufficient materials were available, but the amino acid composition of M-histatin 3 was nearly identical to that of the N-terminal 20 amino acid residues of M-histatin 1. There appears to be only one major histatin in macaque parotid secretion in contrast to the family of histatins in human parotid and submandibular secretions, and the significance of this in the context of evolution and mechanism of action in anticandidal assays is discussed.


1987 ◽  
Vol 42 (3) ◽  
pp. 225-230 ◽  
Author(s):  
Gerd Gäde

Nauphoeta cinerea corpora cardiaca contain peptide material which is capable of eliciting strong hypertrehalosaemia (maximum increase: 27 mg carbohydrates/ml haemolymph) and fat body glycogen phosphorylase-activation (maximal: 70% of the total phosphorylase activity in the a-form) in the American cockroach, Periplaneta americana. It appears that comparable amounts of bioactive material are stored in the corpora cardiaca of N. cinerea and P. americana. Purifica­tion of a methanolic extract of corpora cardiaca from N. cinerea by reversed-phase HPLC revealed that the hypertrehalosaemic phosphorylase-activating activity is concentrated in a single peak. The amino acid composition of the purified neuropeptide material was determined after acid hydrolysis with HCl and methanesulfonic acid. The analyses demonstrated that the N. cinerea hypertrehalosaemic factor is a decapeptide which contains the following amino acid residues: Asp, Thr, Ser, Glu, Pro, Gly (2), Val, Phe, and Trp.


2021 ◽  
Vol 11 (21) ◽  
pp. 10452
Author(s):  
Mohamed Abdelfattah Maky ◽  
Takeshi Zendo

Bioactive peptides were successfully produced from fish (Gadidae) and beef skeletal muscles after being hydrolyzed for 8 h with pepsin. Subsequently, they were purified using a Sep-Pak C18 cartridge and reversed-phase high-performance liquid chromatography (RP-HPLC). The molecular weights of pure fish and beef peptides were determined to be 2364.4 and 3771.8, respectively. According to Edman degradation, the fish peptide was composed of 21 amino acid residues (F21), while the beef peptide was composed of 34 amino acid residues (B34). F21 and B34 displayed angiotensin-converting enzyme inhibitory activity with a half maximal inhibitory concentration (IC50) values of 7.3 µg/mL and 5.8 µg/mL, respectively. F21 exhibited antioxidant activity with an IC50 value of 389.9 µg/mL, whereas B34 exhibited no antioxidant activity. Moreover, F21 and B34 displayed antimicrobial effects against a wide spectrum of food-borne pathogens and spoilage bacteria. Bioactive peptides derived from muscle proteins are a promising strategy for the production of functional food materials and safe food preservatives.


2021 ◽  
Vol 88 (1-2) ◽  
pp. 19-22
Author(s):  
O. P. Balazh

Objective. To investigate serum amino acid pool changes in patients with liver cirrhosis. Materials and methods. 95 patients with liver cirrhosis were participated in the study. In the 1st group (class A disease severity according to Child- Pugh score) there were 18 (18.95%) patients, in the 2nd group (class B) - 25 (26.3%), in the 3rd groups (class C) - 52 (54.7%) patients. The amount of free amino acids in blood serum was determined by reversed-phase high-performance liquid chromatography in isocratic elution mode with electrochemical detection. Results. Violations of free amino acid reserves were revealed in patients with cirrhosis of the liver with a predominant accumulation of aromatic amino acids: phenylalanine - (162.45 ± 14.12) nmol/ml, tyrosine - (99.05 ± 10.07) nmol/ml, tryptophan - (76.10 ± 12.40) nmol/ml, as well as an increase in the content of proline, lysine, cysteine (p <0.05) . In parallel, the decreasing of free serum amino acids with branched side chain levels were observed: valine - up (150.10 ± 8.92) nmol/ml leucine - up (75.14 ± 5.12) nmol/ml (p < 0.05) and isoleucine - up to (80.40 ± 8.01) nmol/ml. Conclusions. The correlation between the second degree of thick guts dysbiosis and increased levels of tryptophan was determined (r = 0.77; p <0.01). III degree thick dysbiosis was correlated with increasing levels of phenylalanine (r = 0.71; p <0.01). In patients of 2nd group the correlations between levels of tryptophan and II degree of intestinal dysbiosis (r = 0.58; p <0.01) and the levels of tyrosine in phenylalanine in III stage intestinal dysbiosis were detected.


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