L-Leucyl-L-alanine
(Synonyms: L-亮氨酸-L-丙氨酸) 目录号 : GC36412
L-Leucyl-L-alanine Hydrate (H-Leu-Ala-OH) is a dipeptide composed of L-leucine and L-alanine joined by a peptide linkage. It is a metabolite.
Cas No.:7298-84-2
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
L-Leucyl-L-alanine Hydrate (H-Leu-Ala-OH) is a dipeptide composed of L-leucine and L-alanine joined by a peptide linkage. It is a metabolite.
| Cas No. | 7298-84-2 | SDF | |
| 别名 | L-亮氨酸-L-丙氨酸 | ||
| 分子式 | C9H18N2O3 | 分子量 | 202.25 |
| 溶解度 | Water: 100 mg/mL (494.44 mM); Methanol: 8.33 mg/mL (41.19 mM) | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 4.9444 mL | 24.7219 mL | 49.4438 mL |
| 5 mM | 0.9889 mL | 4.9444 mL | 9.8888 mL |
| 10 mM | 0.4944 mL | 2.4722 mL | 4.9444 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Site of intestinal dipeptide hydrolysis
J Physiol 1977 Dec;273(3):731-43.PMID:604456DOI:10.1113/jphysiol.1977.sp012120.
1. Sacs of everted small intestine of the hamster have been used to study the site of final hydrolysis of twelve dipeptides. 2. The results suggest that L-alanyl-glycine, glycyl-glycine, L-valyl-L-valine, L-alanyl-L-valine, L-valyl-L-alanine and L-prolyl-glycine are hydrolysed beyond the locus of the active transport mechanism for D-glucose, perhaps even within the cell. These may be designated class 1 (deep) dipeptides. 3. In contrast, superficial (perhaps even surface) hydrolysis seems to occur with L-alanyl-L-alanine, L-leucly-L-leucine, glycyl-L-alanine, L-alanyl-L-leucine, L-Leucyl-L-alanine and glycyl-L-proline. These may be designated class 2 (superficial) dipeptides. 4. All the dipeptides were able to partially inhibit D-glucose active transport, the findings supporting the view that more than one mechanism may exist for the active absorption of the sugar.
The responses of rat intestinal brush border and cytosol peptide hydrolase activities to variation in dietary protein content: dietary regulation of intestinal peptide hydrolases
J Clin Invest 1974 Oct;54(4):890-8.PMID:4430719DOI:10.1172/JCI107828.
The effects of variation in dietary protein content on small intestinal brush border and cytosol peptide hydrolase activities have been investigated. One group of rats was fed a high protein diet (55% casein) and another group was fed a low protein diet (10% casein). After 1 wk, brush border peptide hydrolase activity (L-leucyl-beta-naphthylamide as substrate) and cytosol peptide hydrolase activity (L-prolyl-L-leucine as substrate) were determined in mucosae taken from the proximal, middle, and distal small intestine. As judged by several parameters, brush border peptide hydrolase activity was significantly greater in rats fed the high protein diet when data for corresponding segments were compared. In contrast, no significant difference was seen in cytosol peptide hydrolase activity. IN A SECOND STUDY, BRUSH BORDER AND CYTOSOL PEPTIDE HYDROLASE ACTIVITIES WERE DETERMINED IN THE PROXIMAL INTESTINE BY UTILIZING AN ADDITIONAL THREE PEPTIDE SUBSTRATES: L-Leucyl-L-alanine, L-phenylalanylglycine, and glycyl-L-phenylalanine. Sucrase, maltase, and alkaline phosphatase activities were also determined. As before, brush border peptide hydrolase activities were significantly greater in rats fed the high protein diet. However, activities of the nonproteolytic brush border enzymes did not vary significantly with diet. In contrast to the results obtained with L-prolyl-L-leucine as substrate for the cytosol enzymes, cytosol activity against the three additional peptide substrates was greater in rats fed the high protein diet. It is suggested that the brush border peptide hydrolase response to variation in dietary protein content represents a functional adaptation analogous to the regulation of intestinal disaccharidases by dietary carbohydrates. The implication of the differential responses of the cytosol peptide hydrolases is uncertain, since little is known of the functional role of these nonorgan-specific enzymes.
Comparison of four different phenylalanine determination methods
Clin Chim Acta 1997 Aug 8;264(1):65-73.PMID:9267704DOI:10.1016/s0009-8981(97)00074-0.
The ISOLAB NCS phenylalanine determination kit has not been widely applied for neonatal screening and patient follow up in Europe until now. This method, based on fluorescence enhancement of a phenylalanine-ninhydrin reaction product by the dipeptide L-Leucyl-L-alanine, was compared with three other procedures: (1) The Quantase kit (Shield Diagnostics) for enzymatic determination of phenylalanine, (2) the standard amino acid analysis by means of ion exchange chromatography, and (3) the Guthrie Test as a bacterial inhibition assay (BIA). Only authentic samples from PKU patients were evaluated: once with the NCS kit and at least once with one of the three other methods. There was good agreement between the results obtained by the NCS kit using dried blood specimens and either of the other three methods, as well as between the NCS kit using plasma samples and the Quantase kit and ion exchange chromatography. Plasma sample measurement by NCS proved advantageous because of the option of measuring each microtiter plate twice by resetting the calibrators, i.e. special standards for plasma samples could be used on the same plate. We conclude that this method should prove time saving and cost effective when both neonatal screening and patient follow up are carried out in the same laboratory.
The reaction of aminoacylase with chloromethylketone analogs of amino acids
Z Naturforsch C Biosci 1977 Sep-Oct;32(9-10):769-76.PMID:145117DOI:10.1515/znc-1977-9-1018.
1. Aminoacylase is irreversibly inactivated by the chloromethylketone analogs of benzyloxy-carobonyl-L-alanine, L-alanine, L-leucine, L-aspartic acid (beta), tosyl-L-phenylalanine and L-Leucyl-L-alanine. The kinetics of the inactivation of the enzyme by the halo-methylketones were investigated. 2. Leucyl-and alanyl chloromethylketone inactivate the enzyme by blocking of 4 SH groups. Experiments with [U-14C]leucyl chloromethylketone confirm that maximal 4 residues are covalently bound to be protein. 3. Inactivation of the enzyme by benzyloxycarbonylalanyl and tosylphenylalanyl chloromethylketone is the result of the substitution of the epsilon-amino group of one lysine resine residue per active site and not of SH groups. However, in the presence of competitive inhibitors these halomethylketones react only with the SH groups of the enzyme, too.
A fluorometric assay for beta-phenylethylamine in human urine
Clin Chim Acta 1977 Aug 1;78(3):401-10.PMID:884865DOI:10.1016/0009-8981(77)90073-0.
A sensitive and specific method for the fluorometric determination of beta-phenylethylamine (PEA) in human urine is described. PEA in urine was separated from phenylalanine and 5-hydroxytryptamine by n-heptane extraction, and determined by the ninhydrin reaction in the presence of L-Leucyl-L-alanine. Using this method, the amounts of free PEA in urine samples of normal subjects and schizophrenics were measured. Normal subjects excreted 15.9 +/- 6.4 microgarm/day of free PEA, and chronic schizophrenics 9.3 +/- 2.7 microgram/day of free PEA. In normal subjects, the highest excretion of free PEA was observed in the period from 4:00 p.m. to 12:00 p.m. in a day.