Anyone know of a lab that does testing of HGH?

[MACKATTACK]

Looking to send some vials out for tesitng. Wondering if anyone knows of a lab that does this type of work. Not even sure if this type of question can be asked. If so I will edit it.

Thanks.

[ppwc1985]

I don't think they do that anymore.

[Sgt. Hartman]

......

There's always a lot of talk on here about people wanting to get their GH tested and recently another board has posted results of several generic GH brands that they paid to have tested at a licensed US facility.

The problem with giving these tests any credibility is that there currently isn't a proper method of testing a recombinant protein based drug for "biological activity". In other words it could test to be pure 191aa GH and have absolutely none of the desired effect when administered. This article is written by Boris Y. Zaslavsky, Department of Physiology and Biophysics, Cornell University Medical College.




Recombinant DNA (rDNA) technology has led to the development of new protein-based drugs that are gaining worldwide regulatory approval. Human growth hormone , human insulin , β- and γ-interferons, and erythropoietin are just a few examples of approved rDNA-derived biopharmaceuticals.

The biological effects, purity, and potency of a drug is governed by the chemical structure of the drug for both traditional drugs and biopharmaceuticals. Standard analytical methodologies used for structural analysis of conventional drugs are, however, inadequate for complete characterization of protein-based products.

Two main reasons for this inadequacy are the large molecular size and conformational flexibility of protein-based drugs. The large molecular size hinders the possibility to detect, for example, repla***ent or chemical modification of a single amino acid residue or a change in a single glycosylation site. These alterations of the biomolecule structure, however, may lead to subtle changes of the molecule conformation resulting in significant changes in the pharmacological properties of the product.

Additionally, the wrong choice of manufacturing conditions or formulation may lead to improperly folded polypeptide chains which are biologically inactive. Hence, further methodologies capable of analysis of the protein conformation are needed.

Currently, the analysis of biopharmaceuticals relies heavily on the use of sophisticated methods for the demonstration of the structural identity, homogeneity and purity of the products. These methods include amino acid and carbohydrate analysis, N- and C-terminal sequence analysis, spectroscopic (UV, CD, ORD) analysis, peptide mapping, electrophoresis, chromatographic purity profile methods, potency/activity assays, etc. It must be emphasized that no one method is considered to be sufficient in itself, and that multiple methods are necessary to completely characterize and/or control such products.

For example, amino acid analysis for proteins with molecular weights above about 16 kilodaltons is known to be of very limited value. While useful for identification of the target protein, N-terminal and C-terminal sequencing only partially characterize the protein. Analysis of the primary structure, however, is insufficient to assure the biological potency of a protein, particularly since the potency depends on the protein conformation.

The conformation of proteins is usually analyzed by optical spectroscopy, such as UV spectroscopy, fluorescence spectroscopy, optical rotary dispersion, or circular dichroism. These methods are generally not sensitive enough to detect the subtle conformational changes caused by small alterations in the protein structure, especially if these changes do not affect side-chain chromophores from tryptophan, phenylalanine, tyrosine, and cysteine residues within the protein. Furthermore, these methods as well as others, such as electrophoresis, isoelectric focusing, differential scanning calorimetry, light scattering, ultracentrifugation, gel filtration, and immunological assays, only provide information about a particular structural or functional feature of a protein.

Chromatography is currently the most widely used analytical method for determining the purity of small organic drugs. Four modes of High-Performance Liquid Chromatography (HPLC) currently used for protein analysis are size-exclusion, ion-exchange, reversed-phase, and hydrophobic interaction chromatography. All these HPLC methods, though commonly employed to monitor the purity of biopharmaceuticals, are usually incapable of resolving proteins that differ by one or two residues or detecting other small changes in the macromolecular structure.

Hence, while chromatography is sufficient for determining whether a small organic drug is functional, the evaluation of a biopharmaceutical requires measurements of biological activity. Many of these measurements are the animal-based assays, particularly when the mechanism of action of the biopharmaceutical is not well defined. These assays are generally imprecise (with variability often 30% to 100%), time-consuming, and costly, and are not rugged. Cell culture assays can be used when the protein-based drug produces a measurable response in a cell-based system. The variability of these assays is much lower, often in the range of 10% to 30% or better (e.g., in vitro clot lysis assay has a variability of about 5%).

Physicochemical tests are much faster, more precise, and more reliable than biological assays. A physicochemical test providing information related to the biological potency of a protein-based drug would improve the control of the safety and efficacy of the drug.

Such a test should meet the following requirements: (1) it should provide information quantitatively related to the biological potency of a biopharmaceutical, (2) it should be capable of detecting minor changes in the structure of large macromolecules, (3) it should be especially sensitive to the structural changes affecting the efficacy of a biomacromolecule, (4) it should be sensitive to the presence of impurities in the product in quantities as small as 0.1 to 0.01 wt. %, (5) it should be simple, precise, and rugged, and (6) it should be time-, labor-, and cost-effective so as not to increase the overall cost of the product. Even if only some of these requirements were met, the test would improve the possibilities for assuring the safety and efficacy of biopharmaceuticals, such as recombinant human growth hormone (rhGH).

Stay away from genetics, they are simply not worth it. Don't be fooled into forum test results when the forum in question is a source board full of fake accounts to push the products with false claims.


The process to produce rHGH is very complicated and the equipment used cost's millions of dollars and many of the generic companies don't have this equipment, this is why to produce rHGH it costs a lot of money due to the expensive equipment need to complete the process. I do know someone who I am in contact with and in one of his first emails to me he describes the process of testing this horomone. I will copy the email so you get more of an understanding. My contact has many titles, he is a Professor of research, Scientific manager, he is head of the Biopharmaceutical Bioprocessing technology centre, Director of Mass spectrometry in clinical pharmacology who provide protein analysis services to commercial and academic clients and also a Doctor



Hi Marcus,


there are some things that we can do, some things that we could do, but that would possibly be too expensive (not worth it) and other things that we cannot do.


Please let me start with the last section:


We absolutely cannot test any substances for their suitability for any purpose, particularly not for their use in a diagnostic, therapeutic and/or recreational purpose, when this invloves administering to a living being (including humans).


Measuring the concentration of the growth hormones is something that is actually not as easy as it might seem. The concentration of the hormone can have two different meanings, it could be the chemical concentration of a compound (this is something that we can measure), it could also be the biological activity of this compound (this would be different, if a certain proportion of this chemical would be biologically inactive, which could happen for a variety of reasons). The latter (measuring the biological activity) is something we cannot do. We can measure the chemical concentration of human growth hormone (or any other growth hormone ), but that would involve the chemical synthesis of an internal standard, followed by a fairly complicated experiment, in which we use chemical scissors (en enzyme called trypsin) to chop the protein into pieces, then we analyse these pieces using a combination of high performance liquid chromatography and mass spectrometry, followed by a computer-intensive analysis of the data. The result of this experiment would be the concentration either in units of mol/l or in units of mg/l (the two are interconvertible). I do not know how the IU (stands for International Units) for growth hormone are defined - this might be a functional (biological) unit (which we cannot measure).


Human growth hormone is a chain of 191 different amino acids. One thing we can do is measure the total molecular weight of the protein in a sample to see, if it corresponds to the molecular weight that would be predicted for a protein containing these 191 amino acids. This experiment detects, if one amino acid was missing or another one was added, in some cases (but not in all cases) even, if an amino acid was replaced with a different one. Another outcome of this experiment would be to see, if other, similar proteins are present in the same sample.


In a different experiment we can check, if a protein in a particular sample is really growth hormone or if it is possibly something completely different, for example egg white protein or milk protein .


For your information, I attach two links to articles about human growth hormone :



Best Wishes

[OnTheSauce]

But if you had the test done.... Showed pure hgh. Then ran it and got bloods done showing elevated igf and growth serum.... You would be good to go