3 مقاله موسسه در مجله نیچر

مواردی از قبیل افزایش تنوع شدید فرآورده ها، همکاری و اجرای طرح های تحقیقاتی مشترک با موسسات مشابه خارجی و نهادهای بین المللی مربوطه نظیر سازمان دامپزشکی جهانی، سازمان بهداشت جهانی، فائو و غیره نمونه هایی از این فعالیتها بوده است. یک موردی که لازم می دانم به موارد قبلی اضافه کنم انتشار مقالات اعضای هیات علمی وقت موسسه در آنزمان در مجلات معتبر علمی است. مجله نیچر که اهل فن با آن کاملا آشنا هستند و هر محققی آرزو دارد که مقاله اش در آن چاپ شود، دارای IF یا ضریب تاثیر 40 و بلکه بیشتر می باشد (توجه داشته باشیم که بهترین ضریب تاثیر مجلات ایرانی سال 2014 میلادی مربوط به ژورنال هپاتیت با ضریب تاثیر 796/1 در JCR می باشد). مجله نیچر در دهه 40 شمسی مقالاتی را از محققین موسسه رازی تحت عنوان بنگاه سرم سازی رازی حصارک به چاپ رسانده است. سه مقاله از آقای دکتر امین و دکتر شاملو با عناوین زیر را می توانید با جستجو در گوگل اسکولار بیابید.

- Amin, A. (1961), 'Comparison of the serum protein fractions of the newly hatched chick with those of adult birds using starch-gel electrophoresis', Nature, 191 (4789), 708.

- Amin, A. (1961), 'Comparison of the serum protein fractions of the developing chicken embryo by the technique of starch-gel electrophoresis', Nature, 192 (4800), 356-57.

- Amin, A. and Shamloo, K. D. (1963), 'Distribution of the serum proteins of syrian hamster as revealed by starch-gel electrophoresis', Nature, 198 (4879), 485-86.

این ها نمونه هایی از اقدامات هیات علمی موسسه در 54 سال پیش هستند که نکاتی را به ما یاد آوری می کنند:

یکی اینکه اعضا کارکنان موسسه با تکنیکهای آزمایشگاهی روز آن زمان نظیر الکتروفورز کار می کرده اند و به اصطلاح از نظر علمی به روز بوده اند بلکه کارهای آزمایشگاهی بهتری هم انجام می داده اند و در واقع در مسیر جریان تولید علمی روز دنیا بودند،

دوم اینکه آزمایشگاه های موسسه به روز بوده اند که این مقالات در آنها تولید می شد،

سوم اینکه ارتباط قوی با دانشگاه ها و مراکز علمی دنیا برقرار بوده است یعنی که تبادل علمی بین موسسه و این مراکز بوده،

و غیره...

توجه داشته باشیم که این مقالات در 54 سال پیش چاپ شده اند یعنی به عبارتی برخی از مسئولین فعلی موسسه در آنزمان هنوز متولد نشده بودند. قصد ندارم ذهن شما را با اینسئوال مغشوش کنم که چرا با وجود افزایش پرسنل، درآمد، بودجه، امکانات و غیره نسبت به آن زمان موسسه رازی قادر به تکرار که نه حتی چاپ یک مقاله در یک ژورنال متوسط علمی دنیا هم نیست؟

 ای که نود رفت و در خوابی--- مگر این چند روزه دریابی

توضیح در باره جناب دکتر امین و دکتر شاملو

بنا به اطلاعاتی که از حافظه ماندگار موسسه رازی جناب آقای رشید دریافت شد جناب دکتر  ابوالقاسم  امین و جناب آقای دکتر شاملو سالها در بخش شیمی موسسه کار می کرده اند. جناب رشید می فرمایند حدود سال 1371 جناب آقای دکتر امین را در خیابان نفت ملاقات کرده اند و در این سال ایشان در آزمایشگاه مادام کوری مشغول فعالیت بوده اند. اطلاعات دیگری در باره این دو چهره نداریم. از کسانی که اطلاعات بیشتری در باره دکتر امین و دکتر شاملو دارند دعوت می کنیم با بنده ( میرافضلی) تماس بگیرند

متن مقالات منتشر شده:

Letters to Nature Nature 191, 708 (12 August 1961); doi:10.1038/191708a0

Comparison of the Serum Protein Fractions of the Newly Hatched Chick with those of Adult Birds using Starch-gel Electrophoresis

 

A. AMIN

  Razi Institute, Hessarak, Karaj, Iran.

IT has been established by several investigators that serum protein components of chick embryo undergo qualitative as well as quantitative changes throughout the developmental period until the time of hatching1–4. The serum protein composition of the newly hatched chick, however, resembles that of the adult bird, as revealed by moving-boundary and paper electro-phoresis. The technique of starch-gel electrophoresis suggested by Smithies5 is promising in that it enables one to detect numerous fractions in the pattern of the serum proteins, particularly in the α- and β-globulin regions, which cannot be detected by the conventional method of Tiselius or paper electrophoresis. By using the starch-gel method, I have been able to demonstrate differences in the patterns of serum proteins of the day-old and week-old chicks when compared with pooled sera of one- and two-year -old roosters, as shown in Fig. 1. The electrophoresis was performed on a vertical tray6 for 18 hr. using borate buffer of pH 8.6 and a field-strength of 6 V./cm. Repeated electrophoretic runs gave patterns similar to those shown in Fig. 1, for the four age groups. Twelve fractions could be distinguished on the patterns of the adult roosters (two pre-albumin components are not seen on the photographs). The same number of fractions could also be seen on the electrophoretic patterns of the young chicks. The mobility and the number of fractions of α-globulins of the newly hatched chicks are distinctly different from those of adult birds. The fraction b of the serum of a day-old chick does not seem to be present in the serum of an adult bird, and of fraction d only traces are observed. Very little γ-globulin is present in day-old and week-old chicks. A distinct narrow band which is immediately behind the albumin (a post-albumin ?) in the adult bird cannot be seen in the young chicks.

  1. Moore, D. H. , Shen, S. H. , and Alexander, C. S. , Proc. Soc. Exp. Biol. Med., 58, 307 (1945). | ISI | ChemPort |
  2. Marshall, M. E. , and Deutch, H. F. , J. Biol. Chem., 185, 155 (1950). | PubMed | ISI | ChemPort |
  3. Hradec, J. , and Lemez, L. , Ceskoslov. Morfol., 2, 260 (1954). | ChemPort |
  4. Vanstone, W. E. , Maw, W. A. , and Common, R. H. , Canad. J. Biochem. Physiol., 33, 891 (1955). | PubMed | ISI | ChemPort |
  5. Smithies, O. , Biochem. J., 61, 629 (1955). | PubMed | ISI | ChemPort |
  6. Smithies, O. , Biochem. J., 71, 385 (1959

 

 

Letters to Nature Nature 192, 356 - 357 (28 October 1961); doi:10.1038/192356b0

Comparison of the Serum Protein Fractions of the Developing Chicken Embryo by the Technique of Starch-Gel Electrophoresis

 

A. AMIN

 

 Razi Institute, Hessarak, Karaj, Iran.

SEVERAL workers have investigated the serum protein composition of the developing chicken embryo, by moving boundary1–3 and paper electrophoresis4,5. The ultracentrifugal analysis of the serum proteins of the early stage of embryonic development of chicken, as investigated by two groups of workers, are not in agreement in regard to the complexity of the molecular structure in that stage1,2. Electrophoretic investigation does show, however, the multiplicity of the components in the early stage, although no complete agreement exists in regard to the number of the components and their relationship to those found in newly hatched and adult birds6. Thus Hradec and Lemez4 reported that the serum proteins of chicken embryo undergo considerable qualitative transformation throughout the development. The technique of starch-gel electrophoresis suggested by Smithies7 enables one to detect in the serum pattern fractions that cannot be observed by other methods of electrophoresis. The pooled sera of five different age-groups of chicken embryo, incubated for 10, 13, 16, 19, and 21 days, were examined by the technique of starch-gel electrophoresis, run simultaneously on the same gel. The electrophoresis was performed on a vertical tray8 for 18 hr., using borate buffer of pH 8.6 and a field-strength of 4 V./cm. Twelve fractions could be distinguished on the pattern of the serum from the embryo aged 21 days, as is shown in Fig. 1 (two pre-albumins are not shown), as was also indicated in ref. 6. At least nine components (except the pre-albumins) could be distinguished on the pattern from the 10-day old chicken embryo, of which at least seven components corresponded in mobility to those found in the day-old chick. The patterns from the sera of 13, 16, and 19 days of incubation also showed similarity in pattern to that of the day-old chick. A component present in the sera of the 10-day and 13-day old embryo and situated somewhere between components h and j of 21-day old embryo was not distinguishable in the sera of the older embryos. The results presented here indicate that apparently with the exception of γ-globulins and some other fractions, as demonstrated in Fig. 1, almost all other components present in the day-old chick are present in the serum of 10-day old embryo, as is revealed by the method of starch-gel electrophoresis, and that the transformation occurring throughout this period of development is apparently of a quantitative rather than qualitative nature.

  1. Moore, D. H. , Shen, S. C. , and Alexander, C. S. , Proc. Soc. Exp. Biol. Med., 58, 307 (1945). | ISI | ChemPort |
  2. Marshall, M. E. , and Deutsch, H. F. , J. Biol. Chem., 185, 155 (1950). | PubMed | ISI | ChemPort |
  3. Heim, W. G. , and Schechtman, A. M. , J. Biol. Chem., 209, 241 (1954). | PubMed | ISI | ChemPort |
  4. Hradec, J. , and Lemez, L. , Czechoslov. Morf., 2, 260 (1954). | ChemPort |
  5. Vanstone, W. E. , Maw, W. A. , and Common, R. H. , Canad. J. Biochem. Physiol., 33, 891 (1955). | PubMed | ISI | ChemPort |
  6. Amin, A. , Nature, 191, 708 (1961). | PubMed | ISI | ChemPort |
  7. Smithies, O. , Biochem J., 61, 629 (1955). | PubMed | ISI | ChemPort |
  8. Smithies, O. , Biochem. J., 71, 585 (1959). | PubMed | ISI | ChemPort |
  9. Amin, A. , and Korour, M. , Embryologia, 7, 1 (1961).

Letters to Nature Nature 198, 485 - 486 (04 May 1963); doi:10.1038/198485a0

Distribution of the Serum Proteins of Syrian Hamster as revealed by Starch-gel Electrophoresis

 

ABOLGHASSEM AMIN & K. D. SHAMLOO

 

 

Laboratoire de Chimie Biologie, Institut D'etat des Serum et Vaccins Razi, Hessarek, Iran.

ALTHOUGH considerable work has been published on the distribution of the serum proteins of various laboratory animals, little has been reported on the electrophoretic pattern of the serum proteins of hamster. Moore1 investigated the serum proteins of several species of animals, including that of the hamster, by moving boundary electrophoresis. He identified six components in the serum of hamster corresponding to albumin, α- and β-globulins and a γ-globulin. Since starch-gel electrophoresis was first suggested by Smithies2, this technique has been applied to the examination of the normal serum proteins of a great many species, including vertebrates3–10, as well as invertebrates11.

  1. Moore, D. H. , J. Biol. Chem., 161, 21 (1945). | ISI | ChemPort |
  2. Stauber, L. A. , Ochs, J. A. , and Coy, N. H. , Exp. Parasitol., 3, 325 (1954). | Article | PubMed | ISI | ChemPort |
  3. Smithies, O. , Biochem. J., 61, 629 (1955). | PubMed | ISI | ChemPort |
  4. Ashton, G. C. , Nature, 170, 824 (1957).
  5. Ashton, G. C. , Nature, 180, 917 (1957). | PubMed | ISI | ChemPort |
  6. Lanter, A. L. , and Zaki, A. H. , Nature, 180, 1366 (1957). | PubMed |
  7. Goodman, M. , Poulik, E. , and Poulik, M. D. , Nature, 188, 79 (1960). | Article | PubMed | ISI | 
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