Lipotropic and Adrenocorticotropic Hormones. Biological Activities of the Carboxyl-Modified Hormones

1974 ◽  
Vol 52 (3) ◽  
pp. 723-726 ◽  
Author(s):  
C. Gilardeau ◽  
M. Chrétien ◽  
M. Lis
Keyword(s):  
Methyl Ester ◽  
Coupling Agent ◽  
Lipolytic Activity ◽  
Biological Activities ◽  
Water Soluble ◽  
Carboxyl Groups ◽  
Glycine Methyl Ester

The carboxyl groups of sheep adrenocorticotropic and beta-lipotropic hormones (ACTH and beta-LPH) were modified by glycine methyl ester and taurine using a water-soluble carbodiimide as a coupling agent. The biological activities of these derivatives were measured and compared with those of the native hormones. With ACTH, the lipolytic activity is almost unaffected although the adrenocorticotropic activity is completely destroyed. LPH partially looses its lipolytic activity.

Sequence Determination of a Protein with N-Terminal Glutamic Acid after Modification of Carboxyl Groups with Carbodiimide as the Coupling Agent

1974 ◽  
Vol 52 (6) ◽  
pp. 560-562
Author(s):  
C. Gilardeau ◽  
M. Chrétien
Keyword(s):  
Methyl Ester ◽  
Glutamic Acid ◽  
Water Soluble ◽  
Carboxyl Groups ◽  
Edman Degradation ◽  
Sequence Determination ◽  
Glutamic Acid Residue ◽  
N Terminus ◽  
Glycine Methyl Ester

Glutamine and asparagine residues in proteins can be differentiated from glutamic and aspartic residues, during the Edman degradation, after modification of the carboxyl groups by glycine methyl ester in presence of a water-soluble carbodiimide. When applied to ovine and porcine beta-lipotropic hormones, which have a glutamic acid residue at the N-terminus, the carbodiimide blocks the N-terminus. However, the Edman degradation proceeds normally, if the phenylthiocarbamyl derivative is formed prior to the modification reaction with glycine. In this communication, radioactive glycine was used to modify the carboxyl groups.

scholarly journals Positive Charges on Lysine Residues of the Extrinsic 18 kDa Protein Are Important to Its Electrostatic Interaction with Spinach Photosystem II Membranes

2005 ◽  
Vol 37 (11) ◽  
pp. 737-742 ◽  
Author(s):  
Jin-Peng Gao ◽  
Zhen-Hua Yong ◽  
Feng Zhang ◽  
Kang-Cheng Ruan ◽  
Chun-He Xu ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Methyl Esters ◽  
Binding Activity ◽  
Water Soluble ◽  
Carboxyl Groups ◽  
Amino Groups ◽  
Charged Amino Acids ◽  
Lysine Residues ◽  
Glycine Methyl Ester ◽  
Positively Charged

Abstract To determine the contribution of charged amino acids to binding with the photosystem II complex (PSII), the amino or carboxyl groups of the extrinsic 18 kDa protein were modified with Nsuccinimidyl propionate (NSP) or glycine methyl ester (GME) in the presence of a water-soluble carbodiimide, respectively. Based on isoelectric point shift, 4–10 and 10–14 amino groups were modified in the presence of 2 and 4 mM NSP, respectively. Similarly, 3–4 carboxyl groups were modified by reaction with 100 mM GME. Neutralization of negatively charged carboxyl groups with GME did not alter the binding activity of the extrinsic 18 kDa protein. However, the NSP-modified 18 kDa protein, in which the positively charged amino groups had been modified to uncharged methyl esters, failed to bind with the PSII membrane in the presence of the extrinsic 23 kDa protein. This defect can not be attributed to structural or conformational alterations imposed by chemical modification, as the fluorescence and circular dichroism spectra among native, GME and NSP-modified extrinsic 18 kDa proteins were similar. Thus, we have concluded that the positive charges of lysyl residues in the extrinsic 18 kDa protein are important for its interaction with PSII membranes in the presence of the extrinsic 23 kDa protein. Furthermore, it was found that the negative charges of carboxyl groups of this protein did not participate in binding with the extrinsic 23 kDa protein associated with PSII membranes.

scholarly journals Relationship between isoelectric point of native and chemically modified insulin and liposomal fusion

1989 ◽  
Vol 264 (1) ◽  
pp. 285-287 ◽  
Author(s):  
R N Farías ◽  
A E López Viñals ◽  
E Posse ◽  
R D Morero
Keyword(s):  
Methyl Ester ◽  
Isoelectric Point ◽  
Carboxyl Groups ◽  
Amino Groups ◽  
Chemically Modified ◽  
Glycine Methyl Ester ◽  
Native Insulin ◽  
Ph Range ◽  
Hydrolysis Of ◽  
Fusion Ability

Native insulin causes fusion of negatively charged liposomes in the pH range from 3.0 to 5.5. In marked contrast, insulin with all three amino groups succinylated did not show fusion ability at any pH. On the other hand, insulin amidated with glycine methyl ester with all six carboxyl groups blocked shifted its activity to higher pH, showing a pH range of activity from 3.0 to 7.4. When the carboxyl groups were recovered by hydrolysis of methoxyl groups from glycine methyl ester-treated insulin, the protein obtained (glycyl-insulin with six free carboxyl groups) behaved as native insulin. A good correlation between the isoelectric point values of insulin and its derivatives and their fusion properties was found.

scholarly journals Interaction of cartilage proteoglycans with hyaluronic acid. The role of the hyaluronic acid carboxyl groups

1977 ◽  
Vol 167 (3) ◽  
pp. 711-716 ◽  
Author(s):  
J E Christner ◽  
M L Brown ◽  
D D Dziewiatkowski
Keyword(s):  
Hyaluronic Acid ◽  
Methyl Ester ◽  
Binding Capacity ◽  
Methyl Esters ◽  
Binding Activity ◽  
Carboxyl Groups ◽  
Nasal Cartilage ◽  
Carboxylate Groups ◽  
Glycine Methyl Ester ◽  
Cartilage Proteoglycans

Hyaluronic acid-derived oligomers of five to fifteen repeat dissaccharides effectively bind to bovine nasal-cartilage proteoglycan and inhibit the interaction between proteoglycans and high-molecular-weight hyaluronic acid. If, however, the hyaluronic acid oligosaccharides are modified by reaction with diazomethane to form the carboxyl methyl esters of the glucuronic acid residues, their inhibitory activity is abolished. The binding capacity can be fully restored by saponification. The amide derivative, which is formed by condensation of the oligosaccharide carboxyl groups with glycine methyl ester, is also ineffective in blocking the proteoglycan-hyaluronic acid interaction. In this case, binding activity is not restored when the amidated oligomers are subjected to saponification to yield the free carboxylate groups on the glycine residues. Thus the displacement of the carboxylate groups on the polysaccharide chain by the interposition of a glycine residue blocks the interaction between the proteoglycans and the hyaluronic acid oligomers. When the oligosaccharide methyl ester is reduced with NaBH4, the resultant glucose-containing oligomers exhibit decreased binding to proteoglycans. Thus it appears that the hyaluronic acid carboxylate anion in a specific spatial orientation is required for hyaluronic acid-proteoglycan interaction.

Synthesis of oxytocin analogues modified in the tripeptide side-chain by condensation of aminoterminal linear hexapeptide with the carboxyterminal tripeptide

1979 ◽  
Vol 44 (1) ◽  
pp. 275-287 ◽  
Author(s):  
Jan Hlaváček ◽  
Tomislav Barth ◽  
Karel Bláha ◽  
Karel Jošt
Keyword(s):  
Methyl Ester ◽  
Side Chain ◽  
Glycine Methyl Ester

For the synthesis of oxytocin (Ia) analogues modified in the carboxyterminal part of the molecule, a method based on the condensation of protected aminoterminal hexapeptide with tripeptides by the action of dicyclohexylcarbodiimide and pentafluorophenol in the presence of 1-hydroxybenzotriazole was devised. Using this method [7-[U-13C]proline]oxytocin (Ib), des-9-glycine-oxytocin (Ic) and methyl ester of oxytocinoic acid ([9-glycine methyl ester]oxytocin) (Id) were prepared.

scholarly journals Analyzing the Carotenoid Composition of Melilot (Melilotus officinalis (L.) Pall.) Extracts and the Effects of Isolated (All-E)-lutein-5,6-epoxide on Primary Sensory Neurons and Macrophages

Molecules ◽  
2021 ◽  
Vol 26 (2) ◽  
pp. 503
Author(s):  
Györgyi Horváth ◽  
Eszter Csikós ◽  
Eichertné Violetta Andres ◽  
Tímea Bencsik ◽  
Anikó Takátsy ◽  
...  
Keyword(s):  
Liquid Chromatography ◽  
Sensory Neurons ◽  
Biological Activities ◽  
Water Soluble ◽  
Soluble Form ◽  
Primary Sensory Neurons ◽  
Isolation And Identification ◽  
Melilotus Officinalis ◽  
Carotenoid Composition ◽  
Anti Inflammatory

Melilotus officinalis is known to contain several types of secondary metabolites. In contrast, the carotenoid composition of this medicinal plant has not been investigated, although it may also contribute to the biological activities of the drug, such as anti-inflammatory effects. Therefore, this study focuses on the isolation and identification of carotenoids from Meliloti herba and on the effect of isolated (all-E)-lutein 5,6-epoxide on primary sensory neurons and macrophages involved in nociception, as well as neurogenic and non-neurogenic inflammatory processes. The composition of the plant extracts was analyzed by high performance liquid chromatography (HPLC). The main carotenoid was isolated by column liquid chromatography (CLC) and identified by MS and NMR. The effect of water-soluble lutein 5,6-epoxide-RAMEB (randomly methylated-β-cyclodextrin) was investigated on Ca2+-influx in rat primary sensory neurons induced by the activation of the transient receptor potential ankyrin 1 receptor agonist to mustard-oil and on endotoxin-induced IL-1β release from isolated mouse peritoneal macrophages. (all-E)-Lutein 5,6-epoxide significantly decreased the percent of responsive primary sensory neurons compared to the vehicle-treated stimulated control. Furthermore, endotoxin-evoked IL-1β release from macrophages was significantly decreased by 100 µM lutein 5,6-epoxide compared to the vehicle-treated control. The water-soluble form of lutein 5,6-epoxide-RAMEB decreases the activation of primary sensory neurons and macrophages, which opens perspectives for its analgesic and anti-inflammatory applications.

scholarly journals Inactivation of chicken muscle enolase by carbodiimide and glycine methyl ester

FEBS Letters ◽  
1982 ◽  
Vol 143 (2) ◽  
pp. 211-212 ◽  
Author(s):  
Gillian A. Russell ◽  
Linda A. Fothergill
Keyword(s):  
Methyl Ester ◽  
Chicken Muscle ◽  
Glycine Methyl Ester

scholarly journals Wound Healing-Promoting and Melanogenesis-Inhibiting Activities of Angelica polymorpha Maxim. Flower Absolute In Vitro and Its Chemical Composition

Molecules ◽  
2021 ◽  
Vol 26 (20) ◽  
pp. 6172
Author(s):  
Su-Yeon Lee ◽  
Kyung-Jong Won ◽  
Do-Yoon Kim ◽  
Mi-Jung Kim ◽  
Yu-Rim Won ◽  
...  
Keyword(s):  
Wound Healing ◽  
Collagen Synthesis ◽  
Biological Activities ◽  
Melanoma Cells ◽  
Skin Wound ◽  
Water Soluble ◽  
Boyden Chamber ◽  
Tetrazolium Salt ◽  
Skin Wound Healing ◽  
Skin Whitening

Angelica polymorpha Maxim. (APM) is used in traditional medicine to treat chronic gastritis, rheumatic pain, and duodenal bulbar ulcers. However, it is not known whether APM has epidermis-associated biological activities. Here, we investigated the effects of APM flower absolute (APMFAb) on responses associated with skin wound healing and whitening using epidermal cells. APMFAb was obtained by solvent extraction and its composition was analyzed by GC/MS. Water-soluble tetrazolium salt, 5-bromo-2′-deoxyuridine incorporation, Boyden chamber, sprouting, and enzyme-linked immunosorbent assays and immunoblotting were used to examine the effects of APMFAb on HaCaT keratinocytes and B16BL6 melanoma cells. APMFAb contained five compounds and induced keratinocyte migration, proliferation, and type IV collagen synthesis. APMFAb also induced the phosphorylations of ERK1/2, JNK, p38 mitogen-activated protein kinase, and AKT in keratinocytes. In addition, APMFAb decreased serum-induced B16BL6 cell proliferation and inhibited tyrosinase expression, melanin contents, and microphthalmia-associated transcription factor expression in α-melanocyte-stimulating hormone-stimulated B16BL6 cells. These findings demonstrate that APMFAb has beneficial effects on skin wound healing by promoting the proliferation, migration, and collagen synthesis of keratinocytes and on skin whitening by inhibiting melanin synthesis in melanoma cells. Therefore, we suggest that APMFAb has potential use as a wound healing and skin whitening agent.

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