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At least 19 recordsLinked to original sources
PubMed2003

Degradation, cyclic adenosine monophosphate production, insulin secretion, and glycemic effects of two novel N-terminal Ala2-substituted analogs of glucose-dependent insulinotropic polypeptide with preserved biological activity in vivo.

Glucose-dependent insulinotropic polypeptide (GIP) has significant potential in diabetes therapy due to its ability to serve as a glucose-dependent activator of insulin secretion. However, its biological activity is severely compromised by the ubiquitous enzyme dipeptidylpeptidase IV (DPP IV), which removes the N-terminal Tyr(1)-Ala(2) dipeptide from GIP. Therefore, 2 novel N-terminal Ala(2)-substituted analogs of GIP, with Ala substituted by 2-aminobutyric acid (Abu) or sarcosine (Sar), were synthesized and tested for metabolic stability and biological activity both in vitro and in vivo. Incubation with DPP IV gave half-lives for degradation of native GIP, (Abu(2))GIP, and (Sar(2))GIP to be 2.3, 1.9, and 1.6 hours, respectively, while in human plasma, the half-lives were 6.2, 7.6, and 5.4 hours, respectively. In Chinese hamster lung (CHL) cells expressing the cloned human GIP receptor, native GIP, (Abu(2))GIP, and (Sar(2))GIP dose-dependently stimulated cyclic adenosine monophosphate (camp) production with EC(50) values of 18.2, 38.5, and 54.6 nmol/L, respectively. In BRIN-BD11 cells, both (Abu(2))GIP and (Sar(2))GIP (10(-13) to 10(-8) mol/L) dose-dependently stimulated insulin secretion with significantly enhanced effects at 16.7 mmol/L compared with 5.6 mmol/L glucose. In obese diabetic (ob/ob) mice, GIP and (Sar(2))GIP significantly increased (1.4-fold to 1.5-fold; P <.05) plasma insulin concentrations, whereas (Abu(2))GIP exerted only minor effects. Changes in plasma glucose were small reflecting the severe insulin resistance of this mutant. The present data show that substitution of the penultimate N-terminal Ala(2) in GIP by Abu or Sar results in analogs with moderately reduced metabolic stability and biological activity in vitro, but with preserved biological activity in vivo.

Alanine↗
PubMed1995

Biological preservation of foods with reference to protective cultures, bacteriocins and food-grade enzymes.

A review is presented on the present status of biological preservation of foods. Recent developments are discussed with respect to underlying mechanisms of inhibition by 'protective' cultures, and special reference is made to lactic acid bacteria (LAB) and their 'food-grade' safety. The role of bacteriocins, their limitations and potentiating role in biological systems, is also addressed. The use of enzymes (e.g. lysozyme) for food preservation is mainly restricted by economic factors, their inactivation by endogenous food components and their limited activity spectrum. Practical applications of protective cultures refer to particular food commodities that either constitute novel systems with respect to packaging and/or composition, or represent special hygienic risks. It is concluded that biological preservation cannot substitute GMP; it, however, offers an additional (and acceptable) processing parameter for improving the safety and assuring the quality of a given food.

Antibiosis↗
PubMed2000

[Contamination through preparation: risk of molecular genetic studies by using biological preservatives for museum collections].

In paleogenetic science, artifacts (i.e. non-authentic DNA sequences) are mainly produced by cryptic contamination with (i) edaphon DNA sequences and/or (ii) human biomolecules derived from the involved researchers and the laboratory equipment. A third, and yet underestimated source of contamination with exogenous nucleic acids is provided by (iii) conservation practices applied to old material. Bone glue has been successfully used from the beginning of the 19th century up to the middle of this century, and comprises a rich source of non-authentic nucleic acids. An unequivocal identification of treated samples remains difficult since bone and the glue used for conservatory purposes bear similar chemical properties. Since the majority of agents used for the preservation of museum collections are of biological origin, the differentiation between contaminated and non-treated samples is required.

Artifacts↗
PubMed1990

Mechanical engineering problems in preserving biological objects by temperature lowering.

Analysis of dangers caused by mechanical refrigerating and liquid nitrogen systems used for low temperature preserving of biological material and safety measures to be adopted. Hazards are caused by moving or protruding parts of the machinery, its hot parts, noise and vibration, work in cold rooms, possible destruction of pressure vessels, refrigerant inflammation or explosion, breathing the refrigerant or its decomposition products, direct contact of the refrigerant with the skin or mucous tissues, depletion of stratospheric ozone or contamination of food-stuffs.

Equipment and Supplies↗
PubMed1994

Short-chain phosphatidylcholines as superior detergents in solubilizing membrane proteins and preserving biological activity.

The solubilization of plasma and organelle membranes by diheptanoylphosphatidylcholine (DHPC) has been studied. This short-chain phosphatidylcholine is shown to act as a mild detergent, solubilizing effectively both kinds of membranes at DHPC concentrations of 10-20 mM (0.5-1%). The size of the resulting mixed protein-lipid-DHPC micelles ranges between 5 and 8 nm. The protein conformation and hence the enzymatic activity are well preserved over a rather large DHPC concentration range (up to 4-5 times the DHPC concentration required for solubilizing the membranes). Evidence is presented that short-chain phosphatidylcholines are superior to most detergents commonly used by biochemists. This is true not only regarding its excellent dispersing power on both phospholipid bilayers (Gabriel & Roberts, 1986) and biological membranes but also as to its capacity to preserve the native protein structure and hence enzymatic activity in the solubilized state. Due to its special properties DHPC lends itself very well not only to membrane solubilization but also to the purification of the solubilized membrane proteins and reconstitution of the proteins into simple lipid bilayers. Concerning the mechanism of membrane solubilization, evidence indicates that DHPC interacts primarily with the lipid bilayer of the membrane and not with the membrane proteins. DHPC solubilizes membranes by being distributed into the lipid bilayer and breaking it up. In the resulting small mixed micelles, the protein remains associated with its preferred intrinsic membrane lipids and is thus stabilized. The protein-intrinsic lipid complex is successfully shielded from unfavorable contacts with H2O by DHPC-intrinsic lipid interactions.

Bacteriochlorophylls↗
PubMed1990

Hexane preserves biological activity of isozymes and DNA.

Live or frozen insects are required for using isozyme and DNA RFLP methods in studies on population structure, systematics and incrimination of sibling species. Difficulty in keeping insects alive or unavailability of liquid nitrogen or dry ice at regular intervals during extended collection trips poses a serious problem. We describe a method for preserving insects in hexane, under field conditions, for isozyme and DNA analysis.

Animals↗
PubMed1977

Radioactive labelling of viruses: an iodination technique preserving biological properties.

An iodination procedure suitable for the radioactive labelling of viruses to be used in biological experiments is described. It is characterized by the addition of carrier protein to small amounts of virus before iodination with chloramine T, the use of low concentrations of chemicals, and a rapid purification of the labelled virus to minimize radiation inactivation. Using this procedure, polyoma virus was labelled to a specific activity 100 times greater than that which can be obtained with tritiated amino acids, while its sedimentation coefficient, buoyant density, decapsidation and hamagglutinating activity remained unaffected. Reduction in infectivity, possibly due to radiation inactivation, was slight. Similar results were obtained with adenovirus.

Adenoviridae↗
PubMed2003

Novel dipeptidyl peptidase IV resistant analogues of glucagon-like peptide-1(7-36)amide have preserved biological activities in vitro conferring improved glucose-lowering action in vivo.

Although the incretin hormone glucagon-like peptide-1 (GLP-1) is a potent stimulator of insulin release, its rapid degradation in vivo by the enzyme dipeptidyl peptidase IV (DPP IV) greatly limits its potential for treatment of type 2 diabetes. Here, we report two novel Ala(8)-substituted analogues of GLP-1, (Abu(8))GLP-1 and (Val(8))GLP-1 which were completely resistant to inactivation by DPP IV or human plasma. (Abu(8))GLP-1 and (Val(8))GLP-1 exhibited moderate affinities (IC(50): 4.76 and 81.1 nM, respectively) for the human GLP-1 receptor compared with native GLP-1 (IC(50): 0.37 nM). (Abu(8))GLP-1 and (Val(8))GLP-1 dose-dependently stimulated cAMP in insulin-secreting BRIN BD11 cells with reduced potency compared with native GLP-1 (1.5- and 3.5-fold, respectively). Consistent with other mechanisms of action, the analogues showed similar, or in the case of (Val(8))GLP-1 slightly impaired insulin releasing activity in BRIN BD11 cells. Using adult obese (ob/ob) mice, (Abu(8))GLP-1 had similar glucose-lowering potency to native GLP-1 whereas the action of (Val(8))GLP-1 was enhanced by 37%. The in vivo insulin-releasing activities were similar. These data indicate that substitution of Ala(8) in GLP-1 with Abu or Val confers resistance to DPP IV inactivation and that (Val(8))GLP-1 is a particularly potent N-terminally modified GLP-1 analogue of possible use in type 2 diabetes.

Amino Acid Substitution↗