Podcasts about polypeptides

References Guerra-intermediary metabolic lecture archives ProcNatl Acad Sci U S A. 2014 Jun 17; 111(24): 8913–8918 Nutrition, Metabolism and Cardiovascular Diseases, 2023-09-01, Volume 33, Issue 9, Pages 1785-1796. Int J Cancer. 2019 Feb 1;144(3):533-544 --- Send in a voice message: https://podcasters.spotify.com/pod/show/dr-daniel-j-guerra/message Support this podcast: https://podcasters.spotify.com/pod/show/dr-daniel-j-guerra/support

Ep. 308: All About Amino Acids In this episode, Stacy and Sarah talk about amino acid supplementation, empty stomaches and how your supplements compete for the attention of protein transports like they're hailing cabs in the big city! Click here to listen in iTunes   If you enjoy the show, please review it in iTunes! The Paleo View (TPV), Episode 308:  All About Amino Acids Intro (0:00) News and Views (0:40) It is almost our 6-year podcast-iversary! We are recording in advance this week because Sarah will be gallivanting around Canada soon. Most all of Sarah's family lives there, and she hasn't been back to visit in two years. She is very excited to have a vacation and visit family! Sarah is excited about this week's topic- she did a lot of research and "nerding out." We got a lot of great feedback on last week's show about Collagen. This week's show is a great sister show to that topic. Listener Question from Tess: "I have heard people talk about amino acid competition, is this is a thing I should keep in mind? I bring it up because I eat lots of bone broth, collagen, eat meat and also take amino acids as supplements (l-glutamine and l-tyrosine). I started melting my brain about trying to take these all separate from one another, but does it matter? I would love to wash my l-tyrosine down with my collagen water in the morning, then support my gut health all day by drinking little bits of l-glutamine with or without meals! Thank for for the show, and I’m not just saying that because I want to suck up to you and get my question answered!!! I truly appreciate the sensible, practical info you both put out. I’m the type of person who really likes to know the WHY!!!" Protein Digestion Occurs in the stomach and first section of the small intestine. This process is driven by hydrochloric acid. Three main enzymes break food proteins into polypeptides. Pepsin, Trypsin, Chymotrypsin. Polypeptides are then broken down into peptides and amino acids by peptidase enzymes. Exopeptidases and Dipeptidases. About 30% of protein is absorbed as peptides, not individual amino acids. These peptides are endocytosed or hydrolyzed inside enterocytes. About 70% of protein is absorbed as amino acids. In the digestive tract are 5 main families of amino acid transporters. Divided by the types/properties of the amino acids they transport. Neutral amino acid transporters transport: alanine, valine, leucine, methionine, phenylalanine, tyrosine, isoleucine, asparagine, threonine, glycine, proline, histidine, serine, glutamine, cysteine, tryptophan. Different members of transporter families have higher affinity for specific amino acids. For example, B0AT1 neutral amino acid transporter transports L-leucine, L-methionine, L-isoleucine, L-valine before it will transport L-asparagine, L-phenylalanine, L-alanine, L-serine before it will transport L-threonine, glycine, L-proline. Cationic/Basic amino acid and cysteine transporters transport: lysine, arginine, histidine, cysteine. Anionic/Acidic amino acid transporters transport: aspartic acid, glutamic acid. Imino acid and glycine transporters transport: proline, hydroxyproline, glycine. beta-Amino acid and taurine transporters transport: beta-alanine, taurine, betaine. Generally, there are multiple pathways for any given amino acid. Amino acids compete for binding with other high-affinity amino acids for each specific transporter. The transporter system is extremely complex. The body may be able to detect which amino acids are available and which the body needs, in order to prioritize amino acids. Generally, 90% of protein we eat is digested and absorbed. 10% will pass through to the large intestine, where it may be digested by bacteria. Low protein diets cause the body to up-regulate transporters. Typically 1.3-10 grams per hour of amino acids can be absorbed. If you eat a complete protein, you don't need to worry about amino acid content. Is there a need for amino acid supplementation? Branched Chain Amino Acids (BCAA) have been shown to improve muscle recovery and performance. If you are working out really heavily, these can benefit. It has to do with what the system can produce and what we can get from food. Glycine is a commonly deficient amino acid. We aren't eating organ meats and similar things like people used to. Supplementing with glycine can be beneficial. Glutamine has compelling science for supplementation. Glutamine deficiency alone can cause leaky gut. If you are supplementing amino acids, you want to be able to absorb them all. Consuming them with food can create a competitive binding situation. Taking amino acids on an empty stomach is usually recommended. 2 hours after a meal or 1 hour before. However, amino acids are absorbed quickly, so this window is probably smaller. We just don't know everything about amino acid absorption and competition. It is a very complex system. Until more is known, you are probably best off sticking with the instructions on the label. Sarah has been trying BCAA during the past week or so. She takes them post-workout right when she gets home. She has been using Kion Branched Chain Amino Acid Tablets. Stacy could notice a difference in her recovery after lifting heavy when she used to take them. She used plain BCAA and it made her water taste like "dirty feet." If you've enjoyed the show, please recommend it to someone who might enjoy it. We love when you share and when you leave reviews for us! Thanks for listening! Real Everything The Paleo Mom References: https://www.researchgate.net/publication/227744279_Intestinal_absorption_of_peptides_through_the_enterocytes https://www.ncbi.nlm.nih.gov/pubmed/18195088 https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1223487/

Intr Bio Fall lec 4: Polypeptides and small molecule separation methods.

Intr Bio Fall lec 4: Polypeptides and small molecule separation methods.

Polypeptides from purified virions of the calf rotavirus (RV) isolate 993/83 and those from the pigeon RV isolate PO-13 comigrated on SDS-polyacrylamide gels. Two polypeptides of 45K and 47K were detected at the position of VP6. Both proteins behaved like authentic VP6 protein with EDTA and heat treatment. RV 993/83 and PO-13 showed identical one-dimensional peptide maps for VP2, and the 45K and 47K proteins. More than 70% of sera from German cattle older than 1 year showed neutralizing serum antibodies to RV 993/83 and RV PO-13

Most mitochondrial proteins are synthesized as precursors in the cytosol and imported through the contact sites between outer and inner mitochondrial membranes. The molecular mechanism of membrane translocation of precursor proteins is largely unclear. For this report, various hybrid proteins between portions of the precursor of cytochrome b2 and the entire dihydrofolate reductase (DHFR) were accumulated in mitochondrial contact sites. We unexpectedly found that about 30 amino acid residues of the polypeptide chain in transit were sufficient to span both membranes. This suggests linear translocation of the polypeptide chain and presents evidence for a high degree of unfolding of polypeptides traversing the mitochondrial membranes.

Fri, 2 Nov 1990 12:00:00 +0100 http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WSN-4C592Y4-6P&_user=616146&_coverDate=11%2F02%2F1990&_rdoc=3&_fmt=high&_orig=browse&_srch=doc-info(%23toc%237051%231990%23999369996%23496577%23FLA%23display%23Volume)&_cdi=7051&_sort=d&_docanchor https://epub.ub.uni-muenchen.de/7604/1/Neupert_Walter_7604.pdf Pfanner, Nikolaus; Craig, Elisabeth A.; Hartl, Franz-Ulrich; Neupert, Walter ddc:610, Medizin

Cloned genomic fragments from the region (0.769 to 0.818 map units) coding for immediate-early (IE) transcripts of murine cytomegalovirus (MCMV) were used to analyze the physical organization of this region, the direction of transcription, and the proteins synthesized in vitro. Three IE transcription units could be identified. From IE coding region 1 (ie1; 0.781 to 0.796 map units) a dominant 2.75-kilobase (kb) RNA was transcribed from right to left on the prototype arrangement of the MCMV genome which directed the synthesis of an 89,000-molecular-weight polypeptide (89K polypeptide), the major IE protein. This phosphoprotein (pp89) has been shown to be active in the regulation of transcription. Upstream of ie1 and separated by the MCMV enhancer sequence was a second IE coding region, ie2, which was mapped at 0.803 to 0.817 map units. From ie2 a 1.75-kb RNA of moderate abundance was transcribed in the direction opposite to that of the ie1 RNA. After hybrid selection of the ie2 transcript, a 43,000-molecular-weight translation product was detected. A third coding region, ie3, was located directly downstream of ie1 (0.773 to 0.781 map units). The series of RNAs with low abundance, terminating in ie3, probably used the ie1 transcription start site and ranged from 1.0 to 5.1 kb in size. The 5.1-kb RNA apparently represents the nonspliced transcript from both coding regions ie1 and ie3. A 15K polypeptide was translated in vitro from RNA that was hybrid selected by ie3 sequences. Immunoprecipitation with monoclonal antibody revealed that 31K to 67K polypeptides were related to pp89. Some of these proteins were translated from RNAs that were smaller than 2.75 kb. Polypeptides related to pp89 were also synthesized in vivo. Because polypeptides unrelated to pp89 that were translated from RNA that was selected by ie2 and ie3 sequences were not immunoprecipitated by murine antisera, we assumed that the amount of these proteins synthesized in vivo during infection was probably very low

The immediate-early (IE) infected cell proteins induced by the murine cytomegalovirus (Smith strain) were studied. These polypeptides were identified as IE proteins by their synthesis in the presence of actinomycin D after removal from a protein synthesis block mediated by cycloheximide. By using a murine antiserum against murine cytomegalovirus, three abundant polypeptides of 89, 84, and 76 kilodaltons (kd) were immunoprecipitated. The three major proteins are phosphorylated but not glycosylated and share antigenic determinants recognized by monoclonal antibodies. The 84 and 76-kd polypeptides represent post-translational modification products of the 89-kd protein. Accordingly, in vitro translation of IE infected cell RNA revealed only the 89-kd polypeptide. The viral origin of the RNA species directing the synthesis of the major 89-kd IE polypeptide was verified by hybrid selection of IE RNA with DNA fragments representing the region from 0.769 to 0.815 map units of the murine cytomegalovirus genome. IE polypeptides were found to be located in the nuclei and the cytoplasm of infected cells. Studies on the kinetics of IE polypeptide synthesis revealed negative regulatory effects on IE gene expression correlated with the synthesis of early proteins.

Tue, 1 Jan 1980 12:00:00 +0100 https://epub.ub.uni-muenchen.de/8324/1/8324.pdf Scriba, Peter